Abiotic Stress Response in Plants -  - E-Book

Abiotic Stress Response in Plants E-Book

0,0
151,99 €

-100%
Sammeln Sie Punkte in unserem Gutscheinprogramm und kaufen Sie E-Books und Hörbücher mit bis zu 100% Rabatt.
Mehr erfahren.
Beschreibung

Understanding abiotic stress responses in plants is critical for the development of new varieties of crops, which are better adapted to harsh climate conditions. The new book by the well-known editor team Narendra Tuteja and Sarvajeet Gill provides a comprehensive overview on the molecular basis of plant responses to external stress like drought or heavy metals, to aid in the engineering of stress resistant crops. After a general introduction into the topic, the following sections deal with specific signaling pathways mediating plant stress response. The last part covers translational plant physiology, describing several examples of the development of more stress-resistant crop varieties.

Sie lesen das E-Book in den Legimi-Apps auf:

Android
iOS
von Legimi
zertifizierten E-Readern

Seitenzahl: 984

Veröffentlichungsjahr: 2016

Bewertungen
0,0
0
0
0
0
0
Mehr Informationen
Mehr Informationen
Legimi prüft nicht, ob Rezensionen von Nutzern stammen, die den betreffenden Titel tatsächlich gekauft oder gelesen/gehört haben. Wir entfernen aber gefälschte Rezensionen.



Table of Contents

Cover

Related Titles

Title Page

Copyright

Dedication

List of Contributors

Foreword

References

Preface

Part I: Abiotic Stresses – An Overview

Chapter 1: Abiotic Stress Signaling in Plants–An Overview

1.1 Introduction

1.2 Perception of Abiotic Stress Signals

1.3 Abiotic Stress Signaling Pathways in Plants

1.4 Conclusions, Crosstalks, and Perspectives

Acknowledgments

References

Chapter 2: Plant Response to Genotoxic Stress: A Crucial Role in the Context of Global Climate Change

2.1 Introduction

2.2 Genotoxic Effects of UV Radiation

2.3 UV-B-Induced DNA Damage and Related Signaling Pathway

2.4 Repair of UV-B-Induced DNA Lesions: The Role of Photolyases

2.5 Contribution of the NER Pathway in the Plant Response to UV Radiation

2.6 Chromatin Remodeling and the Response to UV-Mediated Damage

2.7 Homologous Recombination and Nonhomologous End Joining Pathways are Significant Mechanisms in UV Tolerance

2.8 UV-B Radiation and Genotoxic Stress:

In Planta

Responses

2.9 Heat Stress: A Challenge for Crops in the Context of Global Climate Change

2.10 Conclusions

References

Chapter 3: Understanding Altered Molecular Dynamics in the Targeted Plant Species in Western Himalaya in Relation to Environmental Cues: Implications under Climate Change Scenario

3.1 Why Himalaya?

3.2 Climate Change is Occurring in Himalaya

3.3 Plant Response to Climate Change Parameters in Himalayan Flora

3.4 Impact on Secondary Metabolism under the Climate Change Scenario

3.5 Path Forward

Acknowledgments

References

Chapter 4: Crosstalk between Salt, Drought, and Cold Stress in Plants: Toward Genetic Engineering for Stress Tolerance

4.1 Introduction

4.2 Signaling Components of Abiotic Stress Responses

4.3 Decoding Salt Stress Signaling and Transduction Pathways

4.4 Drought Stress Signaling and Transduction Pathways

4.5 Cold Stress Signaling and Transduction Pathways

4.6 Transgenic Approaches to Overcome Salinity Stress in Plants

4.7 Conclusion

References

Chapter 5: Intellectual Property Management and Rights, Climate Change, and Food Security

5.1 Introduction: What Are Intellectual Properties?

5.2 Protection of Biotechnologies

5.3 Management Challenges of Biotechnologies

5.4 Making Biotechnologies Available

5.5 Licensing of Biotechnologies

5.6 Intellectual Property Management and Technology Transfer System at Michigan State University

5.7 IP Management and Technology Transfer at Michigan State University

5.8 Enabling Environment for IP Management, Technology Transfer, and Commercialization at MSU

5.9 International Education, Training and Capacity Building Programs in IP Management and Technology Transfer

5.10 Impacts of MSU's IP Management and Technology Transfer Capacity Building Programs

5.11 Summary and Way Forward

References

Part II: Intracellular Signaling

Chapter 6: Abiotic Stress Response in Plants: Role of Cytoskeleton

6.1 Introduction

6.2 Role of Cytoskeleton in Cells

6.3 Abiotic Stress-Induced Structural Changes in MTs

6.4 Abiotic Stress-Induced Structural Changes in MFs

6.5 Abiotic Stress-Induced Structural Changes in Intermediate Filaments

6.6 Abiotic Stress and Cytoskeletal Associated Proteins

6.7 Future Perspectives

Acknowledgments

References

Chapter 7: Molecular Chaperone: Structure, Function, and Role in Plant Abiotic Stress Tolerance

7.1 Introduction

7.2 Heat Shock Proteins

7.3 Calnexin/Calreticulin

7.4 Cyclophilin and Protein Disulfide Isomerase

7.5 Other Reports Regarding Molecular Chaperones

7.6 Conclusion and Future Outlook

Acknowledgment

References

Chapter 8: Physiological Roles of Glutathione in Conferring Abiotic Stress Tolerance to Plants

8.1 Introduction

8.2 Biosynthesis and Metabolism of Glutathione

8.3 Roles of Glutathione under Abiotic Stress Conditions

8.4 Glutathione and Oxidative Stress Tolerance

8.5 Involvement of Glutathione in Methylglyoxal Detoxification System

8.6 Role of Glutathione as a Signaling Molecule under Abiotic Stress Condition

8.7 Conclusion and Future Perspective

Acknowledgments

References

Chapter 9: Role of Calcium-Dependent Protein Kinases during Abiotic Stress Tolerance

9.1 Introduction

9.2 Classification of CDPKs

9.3 Substrate Recognition

9.4 Mechanism of Regulation of CDPKs

9.5 Subcellular Localization of CDPKs

9.6 Crosstalk between CDPKs and MAPKs

9.7 CDPK in Stress Response

9.8 Conclusion

References

Chapter 10: Lectin Receptor-Like Kinases and Their Emerging Role in Abiotic Stress Tolerance

10.1 Introduction

10.2 Evolution of RLKs

10.3 Lectin Receptor-Like Kinase

10.4 Classification of the LecRLK Family

10.5 Roles of LecRLKs

10.6 Conclusion

Acknowledgments

References

Part III: Extracellular or Hormone-Based Signaling

Chapter 11: Heavy-Metal-Induced Oxidative Stress in Plants: Physiological and Molecular Perspectives

11.1 Background and Introduction

11.2 ROS and Oxidative Stress: Role of Heavy Metals

11.3 Heavy-Metal Hyperaccumulation and Hypertolerance

11.4 Molecular Physiology of Heavy-Metal Tolerance in Plants

11.5 Future Perspectives

References

Chapter 12: Metallothioneins and Phytochelatins: Role and Perspectives in Heavy Metal(loid)s Stress Tolerance in Crop Plants

12.1 Introduction

12.2 Methods/Processes of Remediation of Soil

12.3 Metal-Binding Ligands of Plants

12.4 Conclusion

Acknowledgments

References

Chapter 13: Plant Response to Arsenic Stress and Role of Exogenous Selenium to Mitigate Arsenic-Induced Damages

13.1 Introduction

13.2 Arsenic and Selenium in Food Crop Plants

13.3 Role of Signaling Molecules in Mitigation of Arsenic and Selenium

13.4 Conclusion and Future Perspectives

References

Chapter 14: Brassinosteroids: Physiology and Stress Management in Plants

14.1 Background and Introduction

14.2 Physiological Roles of BRs

14.3 Brassinosteroids in Abiotic Stress Tolerance

14.4 Conclusion

References

Chapter 15: Abscisic Acid (ABA): Biosynthesis, Regulation, and Role in Abiotic Stress Tolerance

15.1 Introduction

15.2 Abscisic Acid Biosynthesis and Signaling

15.3 Abscisic Acid and Transcription Factors in Abiotic Stress Tolerance

15.4 Abiotic Stress Tolerance Mediated by Abscisic Acid

15.5 Conclusion and Future Outlook

Acknowledgments

References

Chapter 16: Cross-Stress Tolerance in Plants: Molecular Mechanisms and Possible Involvement of Reactive Oxygen Species and Methylglyoxal Detoxification Systems

16.1 Introduction

16.2 Perception of Heat- and Cold-Shock and Response of Plants

16.3 Reactive Oxygen Species Formation under Abiotic Stress in Plants

16.4 Reactive Oxygen Species Scavenging and Detoxification System in Plants

16.5 Antioxidant Defense Systems and Cross-Stress Tolerance of Plants

16.6 Methylglyoxal Detoxification System (Glyoxalase System) in Plant Abiotic Stress Tolerance and Cross-Stress Tolerance

16.7 Signaling Roles for Methylglyoxal in Induced Plant Stress Tolerance

16.8 The Involvement of Antioxidative and Glyoxalase Systems in Cold- or Heat-Shock-Induced Cross-Stress Tolerance

16.9 Hydrogen Peroxide (H

2

O

2

) and Its Role in Cross-Tolerance in Plants

16.10 Regulatory Role of H

2

O

2

during Abiotic Oxidative Stress Responses and Tolerance

16.11 H

2

O

2

: A Part of Signaling Network

16.12 Involvement of Heat- or Cold-Shock Protein (HSP or CSP) Chaperones

16.13 Amino Acids (Proline and GB) in Abiotic Stress Tolerance and Cross-Stress Tolerance

16.14 Involvement of Ca

+2

and Plant Hormones in Cross-Stress Tolerance

16.15 Conclusion and Future Perspective

Acknowledgments

References

Part IV: Translational Plant Physiology

Chapter 17: Molecular Markers and Crop Improvement

17.1 Introduction

17.2 Molecular Markers

17.3 Conclusion

References

Chapter 18: Polyamines in Stress Protection: Applications in Agriculture

18.1 Challenges in Crop Protection against Abiotic Stress: Contribution of Polyamines

18.2 Polyamine Homeostasis: Biosynthesis, Catabolism and Conjugation

18.3 Drought Stress and PA Metabolism

18.4 Polyamine Metabolism in Drought-Tolerant Species

18.5 Regulation of PA Metabolism by ABA

18.6 Future Perspectives

Acknowledgments

References

Index

End User License Agreement

Pages

xvii

xviii

xix

xx

xxi

xxii

xxiii

xxv

xxvi

xxvii

xxviii

xxix

1

3

4

5

6

7

8

9

10

11

12

13

14

15

16

17

18

19

20

21

22

23

24

25

26

27

28

29

30

31

32

33

34

35

36

37

38

39

40

41

42

43

44

45

46

47

48

49

50

51

52

53

55

56

57

58

59

60

61

62

63

64

65

66

67

68

69

70

71

72

73

74

75

76

77

78

79

80

81

82

83

84

85

86

87

88

89

90

91

92

93

94

95

96

97

98

99

100

101

102

103

104

105

107

108

109

110

111

112

113

114

115

116

117

118

119

120

121

122

123

124

125

126

127

128

129

131

132

133

134

135

136

137

138

139

140

141

142

143

144

145

146

147

148

149

151

152

153

154

155

156

157

158

159

160

161

162

163

164

165

166

167

168

169

170

171

172

173

174

175

176

177

178

179

181

182

183

184

185

186

187

188

189

190

191

192

193

194

195

196

197

198

199

200

201

202

203

204

205

206

207

208

209

210

211

212

213

214

215

216

217

219

220

221

222

223

224

225

226

227

228

229

230

231

233

234

235

236

237

238

239

240

241

242

243

244

245

246

247

248

249

250

251

252

253

254

255

256

257

258

259

260

261

262

263

264

265

266

267

268

269

270

271

272

273

274

275

276

277

278

279

280

281

282

283

284

285

286

287

288

289

290

291

292

293

294

295

296

297

298

299

300

301

302

303

304

305

306

307

308

309

311

312

313

314

315

316

317

318

319

320

321

322

323

324

325

326

327

328

329

330

331

332

333

334

335

336

337

338

339

340

341

342

343

344

345

346

347

348

349

350

351

352

353

354

355

356

357

358

359

360

361

362

363

364

365

366

367

368

369

370

371

372

373

374

375

377

379

380

381

382

383

384

385

386

387

388

389

390

391

392

393

394

395

396

397

398

399

400

401

402

403

404

405

407

408

409

410

411

412

413

414

415

416

417

418

419

420

421

422

423

424

Guide

Cover

Table of Contents

Foreword

Preface

Part I: Abiotic Stresses – An Overview

Begin Reading

List of Illustrations

Chapter 3: Understanding Altered Molecular Dynamics in the Targeted Plant Species in Western Himalaya in Relation to Environmental Cues: Implications under Climate Change Scenario

Figure 3.1 Map of the Himalaya and Greater Hindu Kush Himalayan region.

Figure 3.2 Temperature and precipitation changes in the Himalaya: (a) annual and season trends of temperature (°C year

−1

, shown in bar) in different ecoregions and (b) biannual and season trends of precipitation (mm year

−1

, shown in bar) in different ecoregions (*

P

≤ 0.05, **

P

≤ 0.10.

Figure 3.3 A mechanism to fix higher CO

2

; one of the major requirements of the high-CO

2

environment. The mechanism has been adopted based on the work at high altitude, which is characterized by the environment of low partial pressure of CO

2

and other gases, and still the net photosynthesis rate is comparable to the plants at lower altitudes. Higher activities of PEPCase, AspAT, and GS at high altitude allow fixation of carbon as well as nitrogen. (Source: Refs. [45–48].) Section 3.3.1 has the details on the mechanism. Asp, aspartate; AspAT, aspartate amino transferase; CS, citrate synthase; Glu, glutamic acid; GOGAT, glutamine:2-oxoglutarate aminotransferase; GS, glutamine synthetase; MDH, malate dehydrogenase; NAD-ME nicotinamide adenine dinucleotide specific, NAD-malic enzyme; OAA, oxaloacetate; PEP, phosphoenolpyruvate; PEPCase, phosphoenolpyruvate carboxylase; and Rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase.

Figure 3.4 An engineered thermostable superoxide dismutase developed for plant species experiencing heat stress and the drought stress (that usually accompanies high temperature). The first-order thermal inactivation kinetics suggests C95A (where cysteine at position 95 was substituted with alanine) to be more thermostable than the WT (wild type).

Figure 3.5 Expression of genes during the period of active growth (PAG), winter dormancy (WD), and dormancy release (DR) for two consecutive years in TAB (apical bud and the associated two leaves) and ML (mature leaves) harvested from field-grown tea bushes. Green and red color indicate down- and upregulation of genes, respectively relative to the average expression over the time course.

Figure 3.6 Diagram showing the relationship between primary and secondary metabolism.

Figure 3.7 Picrosides biosynthetic pathway in

Picrorhiza kurroa

as influenced by temperature change. Numerals in parenthesis indicate fold change in gene expression at 15 °C as compared with 25 °C based on reads per exon kilobase per million (RPKM) values. Picrosides are iridoid glycosides derived from cyclization of geranyl pyrophosphate (GPP) to iridoid moiety. Glucose and cinnamate/vanillate convert iridoid into picroside I and picroside II. These steps involve series of hydroxylation and glycosylation reactions catalyzed by cytochrome P450 and glycosyltransferases. GPP can be derived from mevalonate (MVA) or 2-

C

-methyl-d-erythritol 4-phosphate (MEP) pathway. Enzymes of MVA pathway are as follows: AACT, acetyl-CoA acetyltransferase; HMGS, 3-hydroxy-3-methylglutaryl-CoA synthase; HMGR, 3-hydroxy-3-methylglutaryl-coenzyme A reductase; MVK, mevalonate kinase; PMK, phosphomevalonate kinase; PMD, diphosphomevalonate decarboxylase. Enzymes of MEP pathway are DXS, 1-deoxy-d-xylulose-5-phosphate synthase; DXR, 1-deoxy-d-xylulose-5-phosphate reductoisomerase; MCT, 2-

C

-methyl-d-erythritol 4-phosphate cytidylyltransferase; CMK, 4-diphosphocytidyl-2-

C

-methyl-d-erythritol kinase; MDS, 2-

C

-methyl-d-erythritol 2,4-cyclodiphosphate synthase; HDS, 4-hydroxy-3-methylbut-2-enyl diphosphate synthase; HDR, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase. Isopentenyl pyrophosphate isomerase (IPPI) catalyzes the isomerization of dimethylallyl pyrophosphate (DMAPP) to IPP whereas conversion of IPP to geranyl pyrophosphate (GPP) is catalyzed by geranyl pyrophosphate synthase (GPS). Enzymes of phenylpropanoid pathway involved in the biosynthesis of cinnamate are PAL, phenylalanine ammonia-lyase; 4-CH, cinnamic acid 4-hydroxylase; 3-CH,

p

-coumarate 3-hydroxylase; and COMT, caffeoyl-CoA 3-

O

methyltransferase. Solid arrows indicate known steps, whereas broken arrows represent unknown intermediates and enzymes.

Figure 3.8 Significantly enriched functional categories observed for the genes over-expressed at 25 °C as compared with those at 15 °C in

P. kurroa

. The

P. kurroa

transcripts were analyzed using the biological networks gene ontology tool (BiNGO), where colored nodes represent the significantly enriched gene ontology (GO) terms with their statistical significance. Node size is proportional to the number of transcripts in each category. Different color shade represents different significance level (white – no significant difference; color scale, yellow,

p

-value = 0.05; orange,

p

-value < 0.0000005).

Figure 3.9 Effect of drought stress and other associated cues on general phenylpropanoid and flavonoid pathway, which are involved in the biosynthesis of catechins and other flavonoids. Arrows on the right side of the gene indicate the change in expression in response to drought stress, abscisic acid, gibberellic acid, and wounding as reported. Arrows pointing upward, downward, and horizontal indicate increase, decrease, and no change in expression, respectively. ANR, anthocyanidin reductase; ANS, anthocyanin synthase; 4CL, 4-coumarate:CoA ligase; C4H, cinnamate 4-hydroxylase; CHI, chalcone isomerase; CHS, chalcone synthase; DFR, dihydroflavonol reductase; F3H, flavanone 3β-hydroxylase; F3′H, flavonoid 3′-hydroxylase; F3′5′H, flavonoid 3′5′-hydroxylase; LAR, leucoanthocyanidin reductase; PAL, phenylalanine ammonia-lyase; and UFGT, UDP-glucose flavonoid 3-

O

-glucosyl transferase.

Chapter 4: Crosstalk between Salt, Drought, and Cold Stress in Plants: Toward Genetic Engineering for Stress Tolerance

Figure 4.1 Salt stress signaling and transduction pathway in plants.

Figure 4.2 Drought and cold stress sensors in plants.

Figure 4.3 ABA-dependent drought stress signaling.

Figure 4.4 ABA-independent cold and drought signaling pathway in plants.

Chapter 6: Abiotic Stress Response in Plants: Role of Cytoskeleton

Figure 6.1 Cellular events associated with the induction of tolerance to abiotic stresses. In this process of adaptation toward stresses, structural reorganization play an important role mainly affecting cytoskeleton, plasma membrane, organelle membranes, and so on. Tools of modern biology are providing new insights to this hitherto, less explored area of stress physiology.

Chapter 7: Molecular Chaperone: Structure, Function, and Role in Plant Abiotic Stress Tolerance

Figure 7.1 Role of molecular chaperones in various signal transduction cascades from different cellular compartments.

Figure 7.2 Heat-shock-proteins-assisted protein folding. HSP70 is required for the proper folding of newly translated polypeptides, their translocation to various cellular compartments, and degradation of misfolded proteins. HSP90 assists in the functioning of HSP70 and also assists the proper functioning of steroid hormone receptors.

Figure 7.3 CNX/CRT cycle in ER lumen and endoplasmic reticulum associated degradation (ERAD) of malfolded proteins. OST (oligosaccharyl transferase) glycosylates the newly translated polypeptide with Glc3Man9GlcNAc2 when it enters the ER lumen. Glucosidase I and II remove the outer two glucose residues, and the monoglucosylated protein becomes the substrates for calnexin (CNX) and calreticulin (CRT). The other member of the CNX/CRT cycle is ERp57, which promotes isomerization and disulfide bond formation of the monoglucosylated protein bound to CNX/CRT. Properly folded proteins are translocated to the golgi apparatus, while misfolded proteins are recognized by EDEM and function as ER-associated degradation (ERAD).

Figure 7.4 Protein disulfide isomerase (PDI) and cyclophilin. PDI is involved in disulfide shuffling and chaperone activity. PDI assists in disulfide bond isomerization by which proteins undergo proper conformation in the endoplasmic reticulum, while cyclophilin assists in peptidyl cis–trans isomerization.

Chapter 8: Physiological Roles of Glutathione in Conferring Abiotic Stress Tolerance to Plants

Figure 8.1 Structure of glutathione (GSH).

Figure 8.2 Biosynthesis of glutathione.

Figure 8.3 Abiotic stress protection mechanism by glutathione in plants.

Figure 8.4 GSH-mediated toxic metal stress alleviation in plant cell; PC, phytochelatin; PCS, phytochelatin synthase; and , → induction of ROS production.

Figure 8.5 The antioxidant defense system and roles of GSH.

Figure 8.6 Roles of glutathione in methylglyoxal detoxification.

Figure 8.7 Schematic representation of GSH-induced signal transmission under abiotic stress condition.

Chapter 9: Role of Calcium-Dependent Protein Kinases during Abiotic Stress Tolerance

Figure 9.1 Domain structure of calcium-dependent protein kinase. CDPKs are monomeric proteins with unique structures consisting of five domains: an amino terminal variable domain, a kinase domain, an autoinhibitory domain, a regulatory domain, and a C-terminal domain of variable length. The autoinhibitory domain is present next to kinase domain, which inhibits the kinase domain in the absence of Ca

2+

. The autoinhibitory domain is followed by the regulatory domain, which contains four Ca

2+

-binding EF hands, the predominant calcium sensor characterized by the presence of conserved Asp or Glu amino acid.

Figure 9.2 “Release of inhibition” model for the activation of calcium-dependent protein kinase or calmodulin-like domain protein kinase by calcium. Kinases undergo conformational changes in response to calcium, which results in an autoinhibitory interaction.

Figure 9.3 CDPK network and their role in different stress conditions.

Chapter 10: Lectin Receptor-Like Kinases and Their Emerging Role in Abiotic Stress Tolerance

Figure 10.1 The different domains in LecRLKs subclasses. (a) L-type LecRLK, (b) G-type LecRLK, and (c) C-type LecRLK. At the N-terminal domain is the signal peptide region, followed by lectin domain of different specificities. The transmembrane region is connected to the lectin and the C-terminal kinase domain by two juxtamembrane regions of either side. At the C-terminal of the kinase domain is a short cytoplasmic tail believed to play a regulatory role in the RLK functioning. The accessory domains in G-type LecRLK could be either EGF or PAN, or domains.

Figure 10.2 Hypothetical model of LecRLKs' mode of action. The membrane-resident LecRLK, upon stress perception, is activated by phosphorylation. The protein further initiates a downstream phosphorylation cascade, which eventually manipulates certain transcription factors, hormonal pathways, and other downstream signaling molecules, which ultimately lead to the stress-tolerant phenotype.

Chapter 11: Heavy-Metal-Induced Oxidative Stress in Plants: Physiological and Molecular Perspectives

Figure 11.1 Pathways for production of reactive oxygen species in plants under abiotic stress.

Figure 11.2 Detoxification of heavy metal (Cd as an example) involving PC in plants.

Chapter 12: Metallothioneins and Phytochelatins: Role and Perspectives in Heavy Metal(loid)s Stress Tolerance in Crop Plants

Figure 12.1 Demonstration of phytoremediation by a plant involving various ways such as phytoextraction, phytostabilization, and phytovolatization.

Figure 12.2 General structure of metallothioneins. (a) Simple classification of metallothioneins. (b) Schematic representation of the typical arrangement of cysteine residues in four different plant metallothioneins based on consensus sequence. Black bold: highly conserved domain; gray: comparatively less conserved domain.

Figure 12.3 Chemical structure of phytochelatin. (Modified from Shukla

et al.

[103].)

Figure 12.4 Heavy metal ions such as Cd can coordinately bind 1–4 sulfur atoms from either single or multiple PC molecules, resulting in amorphous complexes.

Figure 12.5 A simple schematic representation of the PC biosynthetic pathway. γ-ECS, γ-glutamyl-cysteine synthetase; GS, glutathione synthetase; PCS, γ-glutamyl-cysteine dipeptidyl transpeptidase/phytochelatin synthase; HM, heavy metal(loid)s.

Figure 12.6 Representation of sequence alignment of PCS protein sequences from selected organisms. Representative members of the plant kingdom (

Arabidopsis

, wheat and

C. demersum

) and fungi (

S. pombe

) are chosen for multiple sequence alignment. Shaded portions show highly conserved regions. Vertical arrows and inverted triangles represent conserved cysteine residues across taxa and specific to plant PCS, respectively. Vertical arrows with horizontal line represent amino acid residues essential for PCS catalytic activity. Star represents cysteine residues specifically present in CdPCS1. (Adapted from Shukla

et al.

[131] with kind permission of Springer Science+Business Media.).

Figure 12.7 Demonstration of chemical structure of synthetic PC (ECs). It possess a normal α-peptide bond between the amino acids. (Modified from Shukla

et al.

[103].).

Chapter 13: Plant Response to Arsenic Stress and Role of Exogenous Selenium to Mitigate Arsenic-Induced Damages

Figure 13.1 A flowchart of As poisoning and detoxification. As(V) competes with phosphate transporter and uncouples the mitochondrial oxidative phosphorylation, and is converted to As(III). Further, As(III) binds to sulfhydryl groups of proteins, affecting their structures, and thus toxifies the plants. The detoxification of As(III) is done by the process of methylation, which leads to the formation of less toxic compounds. Oxidative stress produced by both As(V) and As(III) is balanced by the action of SOD, CAT, GPX, and APX. Hydroxyl radical is produced via the Fenton and Haber–Weiss reactions under oxidative stress.

Figure 13.2 Selenate upon activation by ATP sulfurylase follows one of the two pathways: (i) nonenzymatically and GSH reductase-mediated reduction to slenide, and (ii) reduction to selenide by APS reductase and sulfite reductase. Selenide (Se

2−

) may also enter the pathway nonenzymatically. Se

2−

is further assimilated into selenoamino acids, selenocysteine (SeCys), and selenomethionine (SeMet). SeCys is formed by the action of Cys synthase. SeMet may be produced from SeCys via Se cystathionine and Se HomoCys. Selenoamino acids are finally incorporated into the protein.

Figure 13.3 A general model of signal perception and its downstream transduction culminating in cellular responses.

Chapter 14: Brassinosteroids: Physiology and Stress Management in Plants

Figure 14.1 Effect of different types of brassinosteroids (EBL and HBL) on seed germination.

Figure 14.2 Effect of different types of brassinosteroids (EBL and HBL) on shoot length.

Chapter 15: Abscisic Acid (ABA): Biosynthesis, Regulation, and Role in Abiotic Stress Tolerance

Figure 15.1 ABA biosynthesis pathway. Pyruvate is the end product of glycolysis, which is converted into isopentenyl diphosphate (IPP) in plastid via glyceraldehyde 3-phosphate as an intermediate. IPP is converted into zeaxanthin and then subsequently into

trans

-violaxanthin, catalyzed by zeaxanthin epoxidase (ZEP). Under high light, a reverse reaction occurs in chloroplasts catalyzed by violaxanthin de-epoxidase (VDE). These C

15

carotenoids are cleaved into xanthoxin, catalyzed by a family of 9-

cis

-epoxycarotenoid dioxygenases (NCED). Xantoxin is translocated into cytosol, where ABA is synthesized via ABA aldehyde.

Figure 15.2 Cis regulatory elements and transcriptional regulation system of ABA-dependent transcription factors involved in abiotic stress signaling. Transcription factors (TFs) such as MYB, MYC, bZIP, NAC, ERF, and DREB/CBF (C-repeat binding factor), are involved in the upregulation of stress-inducible genes via an ABA-dependent or -independent manner.

Figure 15.3 ABA-mediated abiotic stress signaling. ABA induces the Ca

+

ions level in the cell, which leads to the activation of protein kinases such as CDPK4 and CDPK11. ABA also induces other protein kinases such as OST1 and SnRK with these CDPKs. These induced protein kinases are involved in the activation of ABA-dependent transcription factors, such as ABI4, ABFs, and ABI5. These TFs induce the expression of abiotic-responsive genes after binding at their corresponding cis regulatory elements.

Chapter 16: Cross-Stress Tolerance in Plants: Molecular Mechanisms and Possible Involvement of Reactive Oxygen Species and Methylglyoxal Detoxification Systems

Figure 16.1 Possible mechanisms of heat- or cold-shock-induced cross-adaptation in plants. Heat- or cold-shock sensors in the cell wall plasma membrane triggers the production of Ca

2+

, ROS, MG, and NO, which in turn alters gene expression, leads to change in membrane fluidity, induces synthesis of osmolyte (proline, glycine betaine (GB), etc.), antioxidant compounds, and stress proteins, and eventually induces the phenomenon of cross-adaptation.

Figure 16.2 Schematic representation of a generalized plant cell depicting major sites and sources of ROS production. (Source: Adapted from Hossain

et al.

[19].) For detailed discussion, see text.

Figure 16.3 Reactive oxygen species detoxification systems in plants. Superoxide produced in different cell organelles is rapidly converted to H

2

O

2

by SOD. H

2

O

2

, in turn, is converted to H

2

O by APX and CAT. The oxidation of AsA caused by ROS or APX leads to the formation of monodehydroascorbate (MDHA) and dehydroascorbate (DHA). MDHA is reduced to AsA by MDHAR with the utilization of NADPH, and DHAR converts DHA to AsA by the utilization of GSH. GR is responsible for recycling of GSSG to GSH at the expense of NADPH. GST and GPX catalyze the GSH-dependent reduction of H

2

O

2

and organic peroxides, including lipid peroxides, to H

2

O or alcohols. Both AsA and GSH serve as chemical scavengers of ROS in nonenzymatic reactions. Abbreviations are defined in the text.

Figure 16.4 Superoxide production (O

2

•−

) by methylglyoxal in chloroplast.

Figure 16.5 Metabolic interactions of AsA- and GSH-based antioxidative system and GSH-based glyoxalase system in plant cells [19]. Dotted lines indicate nonenzymatic reactions.

Figure 16.6 Phenotypic appearance of mustard seedlings induced by cold shock-under salt- and drought-stress conditions. Seedlings were subjected to drought stress (induced by 20% PEG-6000) with or without cold pretreatment (6 °C for 5.5 h) (a). Seedlings were subjected to salt stress (150 mM NaCl, 48 h) with or without cold pretreatment (6 °C for 5.5 h) (b).

Figure 16.7 Phenotypic appearance of mustard seedlings induced by heat-shock-under salt- and drought-stress conditions. Seedlings were subjected to salt stress (150 mM NaCl, 48 h) with or without heat-shock (42 °C for 5 h) pretreatment (a). Seedlings were subjected to drought stress (induced by 20% PEG-6000) with or without heat-shock (42 °C for 5 h) pretreatment (b).

List of Tables

Chapter 3: Understanding Altered Molecular Dynamics in the Targeted Plant Species in Western Himalaya in Relation to Environmental Cues: Implications under Climate Change Scenario

Table 3.1 Floral diversity in the Himalaya

Chapter 5: Intellectual Property Management and Rights, Climate Change, and Food Security

Table 5.1 Royalty distribution rates at Michigan State University

Chapter 6: Abiotic Stress Response in Plants: Role of Cytoskeleton

Table 6.1 Various mutant/transgenic plants developed by changes in various cytoskeleton-related genes

Chapter 8: Physiological Roles of Glutathione in Conferring Abiotic Stress Tolerance to Plants

Table 8.1 Roles of exogenous GSH application in abiotic stress tolerance

Table 8.2 State of GSH and other antioxidants and their effects on oxidative stress under different abiotic stress conditions

Table 8.3 Involvement of GSH in quenching ROS in antioxidant defense system

Chapter 9: Role of Calcium-Dependent Protein Kinases during Abiotic Stress Tolerance

Table 9.1 Consensus motifs phosphorylated by CDPKs in

Arabidopisis.

Chapter 10: Lectin Receptor-Like Kinases and Their Emerging Role in Abiotic Stress Tolerance

Table 10.1 Summary of studies carried out on stress-responsive LecRLKs

Chapter 12: Metallothioneins and Phytochelatins: Role and Perspectives in Heavy Metal(loid)s Stress Tolerance in Crop Plants

Table 12.1 Properties of transgenic plants expressing different types of metallothioneins derived from diverse organisms

Table 12.2 Phenotype of transgenic plants expressing diverse PCSs under different heavy metal(loid)s stress

Chapter 16: Cross-Stress Tolerance in Plants: Molecular Mechanisms and Possible Involvement of Reactive Oxygen Species and Methylglyoxal Detoxification Systems

Table 16.1 Example of heat- and cold-shock-induced cross-tolerance in plants

Related Titles

Jenks, M.A., Wood, A.J. (eds.)

Genes for Plant Abiotic Stress

2010

Print ISBN: 978-0-813-81502-2; also available in electronic formats

 

Shinozaki, K., Yoshioka, K. (eds.)

Signal Cross Talk in Plant Stress Responses

2009

Print ISBN: 978-0-813-81963-1; also available in electronic formats

 

Jenks, M.A., Hasegawa, M.M. (eds.)

Plant Abiotic Stress, Second Edition

2nd Edition

2014

Print ISBN: 978-1-118-41217-6; also available in electronic formats

 

Hirt, H. (ed.)

Plant Stress Biology

From Genomics to Systems Biology

2010

Print ISBN: 978-3-527-32290-9; also available in electronic formats

 

Tuteja, N., Gill, S.S., Tiburcio, A.F., Tuteja, R. (eds.)

Improving Crop Resistance to Abiotic Stress

2012

Print ISBN: 978-3-527-32840-6; also available in electronic formats

 

Tuteja, N., Gill, S.S., Tuteja, R. (eds.)

Improving Crop Productivity in Sustainable Agriculture

2013

Print ISBN: 978-3-527-33242-7; also available in electronic formats

 

Tuteja, N., Gill, S.S. (eds.)

Climate Change and Plant Abiotic Stress Tolerance

2014

Print ISBN: 978-3-527-33491-9; also available in electronic formats

Edited by Narendra Tuteja and Sarvajeet S. Gill

Abiotic Stress Response in Plants

 

 

 

 

The Editors

Dr. Narendra Tuteja

International Center for Genetic Engineering and Biotechnology

Aruna Asaf Ali Marg

110 067 New Delhi

India

and

Amity Institute of Microbial Technology

Amity University

E-2 Block, 4th Floor

Room 404A, Sector 125 NOIDA

201313 Uttar Pradesh

India

Dr. Sarvajeet S. Gill

Stress Physiology & Molecular Biology Lab

Centre for Biotechnology

Maharshi Dayanand University

Rohtak - 124 001

Haryana

India

All books published by Wiley-VCH are carefully produced. Nevertheless, authors, editors, and publisher do not warrant the information contained in these books, including this book, to be free of errors. Readers are advised to keep in mind that statements, data, illustrations, procedural details or other items may inadvertently be inaccurate.

Library of Congress Card No.: applied for

British Library Cataloguing-in-Publication Data

A catalogue record for this book is available from the British Library.

Bibliographic information published by the Deutsche Nationalbibliothek

The Deutsche Nationalbibliothek lists this publication in the Deutsche Nationalbibliografie; detailed bibliographic data are available on the Internet at <http://dnb.d-nb.de>.

© 2016 Wiley-VCH Verlag GmbH & Co. KGaA, Boschstr. 12, 69469 Weinheim, Germany

All rights reserved (including those of translation into other languages). No part of this book may be reproduced in any form – by photoprinting, microfilm, or any other means – nor transmitted or translated into a machine language without written permission from the publishers. Registered names, trademarks, etc. used in this book, even when not specifically marked as such, are not to be considered unprotected by law.

Print ISBN: 978-3-527-33918-1

ePDF ISBN: 978-3-527-69459-4

ePub ISBN: 978-3-527-69458-7

Mobi ISBN: 978-3-527-69460-0

oBook ISBN: 978-3-527-69457-0

Cover Design Adam Design, Weinheim, Germany

Dedication

Sanjaya Rajaram was born in 1943 near a small farming village in the state of Uttar Pradesh in northeastern India. He did his BS in Agriculture in 1962 at College of Jaunpur at the University of Gorakhpur. He then studied genetics and plant breeding under Dr M.S. Swaminathan at the Indian Agricultural Research Institute in New Delhi, graduating with his master's degree in 1964. The following year he went to Australia where he studied his PhD in plant breeding at the University of Sydney on a scholarship from the Rotary Club of Narrabri. His Professor and mentor at the university was Dr I.A. Watson, who had been a fellow graduate student with Norman Borlaug under Dr E.C. Stakman at the University of Minnesota. Watson recommended him to Dr Borlaug and Dr Glenn Anderson at the International Maize and Wheat Improvement Center (CIMMYT) in Mexico - and this set in motion Rajaram's distinguished scientific career in wheat research. He implemented a major expansion of Borlaug's ingenious shuttle-breeding approach in countries beyond Mexico, emphasizing wide adaptation of new plants to differing climate and soil conditions; superior grain quality; and increasing the resistance to diseases and pests that had devastated farmers' crops.

Rajaram significantly advanced his mentor's work in improving wheat varieties during a period that has been described as the “golden years” of wheat breeding and production. Like Borlaug, Rajaram had the extraordinary ability to visually identify and select for cross breeding the plant varieties possessing a range of desired characteristics, an ability that was essential to wheat breeding in the 1980s and 1990s. The yield potential of Rajaram's new cultivars increased 20% to 25%. Realizing the importance of freely sharing knowledge to provide developing countries with the ability to produce more food, Rajaram launched efforts to expand the global scientific wheat network – a worldwide exchange of genetic resources, information, and innovations among researchers – which had not been done before. This led to the accelerated development and worldwide spread of high-yielding wheat varieties, which kept the expansion of global wheat production ahead of population growth and made wheat even more accessible to the world's poor. He also realized the importance of nutrition to the poor and strongly supported research on micronutrient-enriched wheat varieties.

After a distinguished career at CIMMYT, Dr Rajaram joined the International Center for Agricultural Research in the Dry Areas and later developed his own seed company, Resource Seeds International.

In 2007, Dr Borlaug expressed high praise for Rajaram in a personal note: “You have developed into the greatest present-day wheat scientist in the world … have made and continue to make many important contributions to further improve world wheat production … have learned to work effectively in many different countries with political leaders of different ideologies … and are a scientist of great vision.”

As the World Food Prize celebrates the centennial year of his mentor, Dr Norman Borlaug, as well as the UN-FAO's International Year of Family Farming, it is especially fitting that the committee recognized the achievements of Dr Sanjaya Rajaram, which have benefitted farmers and consumers worldwide. Dr Rajaram's crossing of winter and spring wheat varieties, which were distinct gene pools that had been isolated from one another for hundreds of years, led to his development of plants that have higher yields and dependability under a wide range of environments around the world.

Dr Sanjaya Rajaram was honored as the 2014 World Food Prize Laureate for his scientific research that led to a prodigious increase in world wheat production – by more than 200 million tons – building upon the successes of the Green Revolution.

His breakthrough breeding technologies have had a far-reaching and significant impact in providing more nutritious food around the globe and alleviating world hunger. Dr Rajaram succeeded Dr Norman Borlaug in leading CIMMYT's wheat breeding program and developed an astounding 480 wheat varieties that have been released in 51 countries on 6 continents and have been widely adopted by small- and large-scale farmers alike.

This book is dedicated to Dr Sanjaya Rajaram for nurturing plant genetics and breeding technologies for providing more nutritious food around the globe and alleviating world hunger.

List of Contributors

 

Rubén Alcázar

University of Barcelona

Departament de Productes Naturals

Biologia Vegetal i Edafologia, Fisiologia Vegetal Unit.

Facultat de Farmacia

Avda de Joan XXIII s/n

08028 Barcelona

Spain

 

Naser A. Anjum

University of Aveiro

Centre for Environmental and Marine Studies (CESAM)

Department of Chemistry

3810-193 Aveiro

Portugal

 

Jayprakash Awasthi

Assam University

Department of Life Science and Bioinformatics

788011 Silchar

Assam

India

 

Alma Balestrazzi

University of Pavia

Department of Biology and Biotechnology `L. Spallanzani'

Via Ferrata 1

27100 Pavia

Italy

 

Renu Bhardwaj

Guru Nanak Dev University

Department of Botanical and Environmental Sciences

143001 Amritsar

Punjab

India

 

Brijmohan Singh Bhau

CSIR-North East Institute of Science and Technology (CSIR-NEIST)

Plant Genomics Laboratory

MAEP Division

785006 Jorhat

Assam

India

 

Munmi Bora

CSIR-North East Institute of Science and Technology (CSIR-NEIST)

Plant Genomics Laboratory

MAEP Division

785006 Jorhat

Assam

India

 

Bitupon Borah

CSIR-North East Institute of Science and Technology (CSIR-NEIST)

Plant Genomics Laboratory

MAEP Division

785006 Jorhat

Assam

India

 

David J. Burritt

University of Otago

Department of Botany

464 Great King Street

Dunedin

New Zealand

 

Daniela Carbonera

University of Pavia

Department of Biology and Biotechnology `L. Spallanzani'

Via Ferrata 1

27100 Pavia

Italy

 

Shuvasish Choudhury

Assam University

Central Instrumentation Laboratory

788011 Silchar

India

 

Mohitosh Dey

Indian Institute of Technology

Department of Biotechnology

Guwahati 781039

India

 

Mattia Doná

University of Pavia

Department of Biology and Biotechnology `L. Spallanzani'

Via Ferrata 1

27100 Pavia

Italy

 

Frederic Erbisch

Intellectual Property Consultant

6036 Harkson Drive

East Lansing

48823 Michigan

USA

 

Masayuki Fujita

Kagawa University

Laboratory of Plant Stress Responses

Department of Applied Biological Science

Faculty of Agriculture

Ikenobe 2393

Miki-cho

Kita-gun

761-0795 Kagawa

Japan

 

Ritu Gill

Centre for Biotechnology

Maharshi Dayanand University

Rohtak

124001 Haryana

India

 

Sarvajeet Singh Gill

Stress Physiology and Molecular

Biology Lab

Centre for Biotechnology

Maharshi Dayanand University

Rohtak

124001 Haryana

India

 

Sneha Gosh

CSIR-North East Institute of Science and Technology (CSIR-NEIST)

Plant Genomics Laboratory

MAEP Division

785006 Jorhat

Assam

India

 

Meetu Gupta

Jamia Millia Islamia

Ecotoxicogenomics Lab

Department of Biotechnology

Jamia Nagar

110025 New Delhi

India

 

Shikha Gupta

Jamia Millia Islamia

Ecotoxicogenomics Lab

Department of Biotechnology

Jamia Nagar

110025 New Delhi

India

 

Dugganaboyana Guru Kumar

CSIR-North East Institute of Science and Technology (CSIR-NEIST)

Plant Genomics Laboratory

MAEP Division

785006 Jorhat

Assam

India

 

Mirza Hasanuzzaman

Kagawa University

Laboratory of Plant Stress Responses

Department of Applied Biological Science

Faculty of Agriculture

Ikenobe 2393

Miki-cho

Kita-gun

761-0795 Kagawa

Japan

 

and

 

Sher-e-Bangla Agricultural University

Department of Agronomy

Faculty of Agriculture

Sher-e-Bangla Nagar

1207 Dhaka

Bangladesh

 

Tom Herlache

MSU Technologies, Michigan State University

325 E. Grand River Ave. Suite 350, East Lansing

48823 Michigan

USA

 

Mohammad Anwar Hossain

Bangladesh Agricultural University

Department of Genetics and Plant Breeding

2202 Mymensingh

Bangladesh

 

Kazi Md. Kamrul Huda

Plant Molecular Biology

International Centre for Genetic Engineering and Biotechnology (ICGEB)

Aruna Asaf Ali Marg

110067 New Delhi

India

 

Manish Kumar

Punjabi University

Department of Botany

147002 Patiala

Punjab

India

 

Sandeep Kumar

Punjabi University

Department of Botany

147002 Patiala

Punjab

India

 

Sanjay Kumar

Biotechnology Division

CSIR-Institute of Himalayan Bioresource Technology

Baijnath Road

176061 (HP) Palampur

India

 

Sanjeev Kumar

Indian Institute of Technology Guwahati

Department of Biosciences and Bioengineering

Guwahati- 781039

India

 

Anca Macovei

International Rice Research Institute (IRRI)

Pili Drive, Los Baños 4031

Laguna

Philippines

 

Karim Maredia

College of Agriculture and Natural Resources

416 Plant and Soil Sciences Building,

1066 Bogue Street, Room 416, East Lansing,

48823 Michigan

USA

 

and

 

Intellectual Property Consultant

6036 Harkson Drive

East Lansing

48824 Michigan

USA

 

Sagarika Mishra

Indian Institute of Technology Guwahati

Department of Biosciences and Bioengineering

781039 Guwahati

India

 

Tapan Kumar Mohanta

National Institute of Plant Genome Research

Aruna Asaf Ali Marg

110067 New Delhi

India

 

Kamrun Nahar

Kagawa University

Laboratory of Plant Stress Responses

Department of Applied Biological Science

Faculty of Agriculture

Ikenobe-2393

Miki-cho

Kita-gun

761-0795 Kagawa

Japan

 

and

 

Sher-e-Bangla Agricultural University

Department of Agricultural Botany

Faculty of Agriculture

Sher-e-Bangla Nagar

1207 Dhaka

Bangladesh

 

Pravendra Nath

CSIR-National Botanical Research Institute

Rana Pratap Marg

226001 Lucknow

India

 

Sanjib Kumar Panda

Assam University

Department of Life Science and Bioinformatics

788011 Silchar

Assam

India

 

Chandana Pandey

Jamia Millia Islamia

Ecotoxicogenomics Lab

Department of Biotechnology

Jamia Nagar

110025 New Delhi

India

 

Prashant K. Pandey

Plant Molecular Biology

International Centre for Genetic Engineering and Biotechnology (ICGEB)

Aruna Asaf Ali Marg

110067 New Delhi

India

 

and

 

Max Planck Institute of Molecular Plant Physiology

Am Mühlenberg 1

D-14476 Potsdam-Golm

Germany

 

Ashwani Pareek

Jawaharlal Nehru University

Stress Physiology and Molecular Biology Laboratory

School of Life Sciences

110067 New Delhi

India

 

Hemanta Kumar Patra

Utkal University

P.G. Department of Botany

Vani Vihar

Bhubaneshwar

751004 Odhisa

India

 

Sangeeta Puri

CSIR-North East Institute of Science and Technology (CSIR-NEIST)

Plant Genomics Laboratory

MAEP Division

785006 Jorhat

Assam

India

 

Callista Rakhmatov

Office of International Research Collaboration, Michigan State University

International Center, 427 N. Shaw Lane, Room 4, East Lansing

48824 Michigan

USA

 

Bedabrata Saha

Indian Institute of Technology Guwahati

Department of Biosciences and Bioengineering

781039 Guwahati

India

 

and

 

Assam University

Department of Life Science and Bioinformatics

788011 Silchar

Assam

India

 

Lingaraj Sahoo

Indian Institute of Technology

Department of Biotechnology

Guwahati 781039

 

Debojit Kumar Sharma

CSIR-North East Institute of Science and Technology (CSIR-NEIST)

Plant Genomics Laboratory

MAEP Division

785006 Jorhat

Assam

India

 

Devesh Shukla

Department of Biology

Western Kentucky University

1906 College Heights

Boulevard

Bowling Green

42101-1080 KY

USA

 

Sneh L. Singla-Pareek

Plant Molecular Biology

International Centre for Genetic Engineering and Biotechnology (ICGEB)

Aruna Asaf Ali Marg

New Delhi 110067

India

 

Alok Krishna Sinha

National Institute of Plant Genome Research

Aruna Asaf Ali Marg

110067 New Delhi

India

 

Geetika Sirhindi

Punjabi University

Department of Botany

147002 Patiala

Punjab

India

 

Neelam Soda

Jawaharlal Nehru University

Stress Physiology and Molecular Biology Laboratory

School of Life Sciences

110067 New Delhi

India

 

Antonio F. Tiburcio

University of Barcelona

Departament de Productes Naturals

Biologia Vegetal i Edafologia, Fisiologia Vegetal Unit.

Facultat de Farmacia

Avda de Joan XXIII s/n

08028 Barcelona

Spain

 

Dipesh Kumar Trivedi

Plant Molecular Biology

International Centre for Genetic Engineering and Biotechnology (ICGEB)

Aruna Asaf Ali Marg

110067 New Delhi

India

 

and

 

Indian Institute of Technology Bombay

Department of Biosciences and Bioengineering

400076 Mumbai

India

 

Prabodh K. Trivedi

CSIR-National Botanical Research Institute

Rana Pratap Marg

Lucknow

UP 226001

India

 

Narendra Tuteja

Plant Molecular Biology

International Centre for Genetic Engineering and Biotechnology (ICGEB)

Aruna Asaf Ali Marg

110067 New Delhi

India

 

and

 

Amity Institute of Microbial Technology

Amity University

E-2 Block, 4th Floor

Room 404A, Sector 125 NOIDA

201313 Uttar Pradesh

India

 

Neha Vaid

Plant Molecular Biology

International Centre for Genetic Engineering and Biotechnology (ICGEB)

Aruna Asaf Ali Marg

110067 New Delhi

India

 

Sawlang Borsingh Wann

CSIR-North East Institute of Science and Technology (CSIR-NEIST)

Biotechnology Division

785006 Jorhat

Assam

India

Foreword

“In a world that has the means for feeding its population, the persistence of hunger is a scandal” [1]. This is a very comprehensive statement made by the UNO and clearly explains the present state of apathy of world agriculture. In the present scenario, crop plants are frequently confronted by various abiotic stresses such as high salinity, drought, low and high temperature, heavy metals, which lead to significant reduction in crop yield. Most commonly abiotic stresses challenge crop plants in combination, for example high temperature stress and drought are commonly encountered by plants and cause unrepairable losses. Global climate change further increasing the frequency of high temperature stress, droughts, and floods, which negatively affect crop yields and pose a serious challenge for global food security. Therefore, protection and increase in crop productivity is now the highest priority worldwide to feed the ever-increasing world population. Recent advances in agriculture biotechnology and the aforementioned agricultural challenges have led to the emergence of high-throughput tools to explore and exploit plant genomes for tolerance toward abiotic stresses. Further, the extent of crop yield loss due to various abiotic stress factors can be reduced by manipulating plant metabolism and using genetically engineered plants.

This book “Abiotic Stress Responses in Plants” edited by Drs Narendra Tuteja and Sarvajeet Singh Gill places a broad picture of plant stress tolerance behavior. The book succeeds in presenting a large variety of concepts, models, and viewpoints and presents a wealth of excellent articles, both broad overviews and detailed accounts, which can broaden our understanding of plant abiotic stress tolerance phenomena. The chapters, written by experts in their respective fields, cover a large array of topics and interpret our recently dramatically enlarged view of the genetic basis of stress-affected plant development, biochemistry, and physiology. This comprehensiveness should make this volume equally valuable not only to basic investigators and application-oriented plant scientists but also to teachers and students entering this field of plant biology. I am sure the readers in the field of agriculture and particularly in abiotic stress management, biotechnology, would find this book very useful. The publisher also deserves congratulations for publishing this useful book.

Prof. M S SwaminathanFounder Chairman,M S Swaminathan Research Foundation,Chennai

References

1. Food and Agricultural Organization (FAO) (2006)

The State of Food Security in the World

, FAO, Rome.

Preface

In the present scenario of frequently changing environmental conditions, abiotic stress factors (salinity, water availability (less or excess water), temperature extremes (freezing, cold, or high), metal/metalloids, nutrient stress, etc.) have become unpredictable and severe menace to the global agricultural productivity. The abiotic stress factors basically restrict crop plants to reach their full genetic potential and cause significant loss to agricultural productivity worldwide. In general, the stress factors are complex and multigenic traits therefore affect the plant performance by significantly inhibiting the growth, development, and finally the produce. In response to the onset of adverse environmental conditions, plants have evolved efficient defense mechanisms by manipulating their tolerance potential through comprehensive defense mechanisms that help them to tolerate stresses through physical adaptation and/or by means of integrated molecular and cellular responses. Perception of stress signals and their transduction is a very crucial step for switching on adaptive responses to ensure the survival of plants. Therefore, understanding the mechanisms by which plants perceive and transduce the stress signals to initiate adaptive responses is essential for engineering stress-tolerant crop plants. Molecular and genomic studies have shown that several genes with various functions are induced by salinity, drought, and cold stresses and that various transcription factors are involved in the regulation of stress-inducible genes. Genetic engineering strategies rely on the transfer of one or several genes that are involved in signaling and regulatory pathways or that encode enzymes present in pathways leading to the synthesis of functional and structural protectants or that encode stress tolerance-conferring proteins.

In this book “Abiotic Stress Response in Plants,” we present a collection of 18 chapters written by experts in the field of abiotic stress signaling and tolerance in plants. This book is an up-to-date overview of current progress in abiotic stress signaling in plants. The various chapters in the book provide a state-of-the-art account of the information available. Following an introduction on “abiotic stress signaling in plants,” the book also discusses how the resulting increase in abiotic stress factors can be dealt with. The result is a must-have hands-on guide, ideally suited for agri-biotechnology, abiotic stress tolerance, academia, and researchers.

For the convenience of readers, the whole book is divided into four major parts:

Part I

:

Abiotic Stresses – An Overview

Part II

:

Intracellular Signaling

Part III

:

Extracellular or Hormone-Based Signaling

Part IV

:

Translational Plant Physiology

Part I: Abiotic Stresses – An Overview covers five chapters (Chapters 1–5). Chapter 1 deals with an introduction to abiotic stress signaling in plants, where emphasis has been placed on understanding the stress signaling and stress responses in plants. Chapter 2 focuses on plant response to genotoxic stress and discusses DNA damage sensing/signaling in relation to UV radiation and high temperature. Chapter 3 covers altered molecular dynamics in plants under changing environmental conditions. Chapter 4 comprehensively deals with crosstalk between salt, drought, and cold stress in plants, where emphasis is on developing strategies for engineering salt tolerance in crop plants. Chapter 5 sheds light on intellectual property management and rights.

Part II: Intracellular Signaling covers five chapters (Chapters 6–10). Chapter 6 discusses the role of cytoskeleton in abiotic stress responses in plants. This chapter deals with specific aspects of the latest advances in our understanding of the plant cytoskeleton and its relation with abiotic stress tolerance. Chapter 7 sheds light on molecular chaperones and their role in abiotic stress tolerance/managements in plants. Chapter 8 discusses the role and importance of glutathione in conferring abiotic stress tolerance in plants. Chapter 9 deals with the role of calcium-dependent protein kinases during abiotic stress tolerance. Chapter 10 also discusses the importance of lectin receptor-like kinases and their emerging role in abiotic stress tolerance.

Part III: Extracellular or Hormone-Based Signaling contains six chapters (Chapters 11–16). Chapter 11 covers the physiological and molecular perspectives of heavy metal–induced oxidative stress in plants, where the basic understanding of heavy metal stress and tolerance in plants has been discussed. Chapter 12 also deals with heavy metal tolerance in plants, pointing out the significance of metallothioneins and phytochelatins. Chapter 13 specifically covers the plant response to arsenic stress. Emphasis has been placed on exploring the role of selenium in overcoming arsenic-induced damages in plants. Chapter 14 discusses the physiology of Brassinosteroids and its significance in stress management in plants. Chapter 15 deals with biosynthesis, regulation, and role of abscisic acid in plant abiotic stress tolerance. Chapter 16 contains information on cross-stress tolerance in plants. This chapter tries to understand the molecular mechanisms and possible involvement of reactive oxygen species and methylglyoxal detoxification systems in stress tolerance.

Part IV: Translational Plant Physiology covers two chapters (Chapters 17 and 18). Chapter 17 focuses on the importance of molecular markers in crop improvement. Chapter 18 discusses the importance of polyamines in stress protection and management, where emphasis has been placed on developing tools that will facilitate the manipulation of polyamine levels in plants and can lead to practical applications in agriculture.

The editors and contributing authors hope that this book will provide a practical update on our knowledge of abiotic stress signaling in plants and will lead to new discussions and efforts to the use of various tools for crop improvement.

We are highly thankful to Dr Ritu Gill, Centre for Biotechnology, MD University, Rohtak, for her valuable help in formatting and incorporating editorial changes in the manuscripts. We would like to thank Prof. M. S. Swaminathan, Founder-Chairman, M S Swaminathan Research Foundation, Third Cross Street, Taramani Institutional Area, Chennai, for writing Foreword and Wiley-VCH Verlag GmbH & Co. KGaA, particularly Gregor Cicchetti, Senior Publishing Editor, Life Sciences; Anne du Guerny, Andreas Sendtko, and Heike Noethe for their support and efforts in the layout. We are also thankful to S. Swapna, Project Manager, MRWs, SPi Global, for her professional support during the typesetting of the book manuscript. We dedicate this book to Dr Sanjaya Rajaram for nurturing plant genetics and breeding technologies for providing more nutritious food around the globe and alleviating world hunger.

EditorsNarendra TutejaICGEB, New DelhiSarvajeet Singh Gill MDU, Rohtak

Part IAbiotic Stresses – An Overview

Chapter 1Abiotic Stress Signaling in Plants–An Overview

Sarvajeet Singh Gill, Naser A. Anjum, Ritu Gill, and Narendra Tuteja

Abstract

Abiotic stress factors [such as salinity, water availability (less or excess water), temperature extremes (freezing, cold, or high), metal/metalloids, nutrient stress, etc.] are basically severe menaces to the global agriculture, restricting the crop plants from reaching their full genetic potential and causing significant yield losses worldwide. In general, stresses are complex and multigenic traits that affect the plant performance significantly by reducing the growth, development, and, finally, the yield. To counteract the adverse effect of the stressors, plant have evolved efficient defense mechanisms by manipulating their tolerance potential through integrated molecular and cellular responses. To face the environmental challenges in the form of various abiotic stresses, perception of stress signals as well as their transduction is a very crucial step for switching on adaptive responses to ensure the survival of plants. Therefore, understanding the physiological and molecular aspects of plant functions under stressful conditions, for example, the activation of cascades of molecular networks (perception of stress signals, transducers, transcription regulators, target stress related genes and metabolites), is desirable. Recent studies have revealed that understanding signal perception and its transduction is crucial for engineering stress tolerance in crop plants. This chapter appraises recent literature on stress signaling and stress responses in plants.

1.1 Introduction

Environmental insults in the form of various abiotic stress factors (salinity, water availability (less or excess water), temperature extremes (freezing, cold, or high), metal/metalloids, nutrient stress, etc.) are basically severe menaces to global agriculture, which restrict the crop plants to reach their full genetic potential and cause significant yield losses worldwide. The changing climatic conditions are further enhancing the severity of abiotic stress, making them even worse. It has been estimated that salinity and/or drought significantly affects >10% of agriculturally cultivable land, which leads to ∼50% reduction in crop productivity globally [1–3]. Stresses are complex and multigenic traits that affect the plant performance significantly by reducing the growth, development, and, ultimately, the final produce. To counteract the adverse effect of environmental insults, plants have evolved efficient defense mechanisms by manipulating their tolerance potential through integrated molecular and cellular responses. In general, the defense machinery involves the activation of stress-inducible genes and their products, which are either functional or regulatory in nature to ascertain direct stress tolerance or through the downstream signal transduction pathway. It is well established that certain stress hormones such as abscisic acid (ABA) also play a pivotal role in the mediation of stress responses in plants. However, plants respond to various stresses through ABA-independent and ABA-dependent pathways [3]. Therefore, it is desirable to understand the physiological and molecular aspects of plant functions under stressful conditions: for example, the activation of cascades of molecular networks (perception of stress signals, transducers, transcription regulators, target stress-related genes, and metabolites). Employing genetic engineering techniques to overcome the load of abiotic stress factors seems to be a promising tool [4]. The present article on abiotic stress signaling in plants focuses on stress signaling and stress responses in plants.

1.2 Perception of Abiotic Stress Signals

Being sessile, plants have to encounter various environmental insults. For their survival, plants have evolved comprehensive defense mechanisms that help them to tolerate stresses through physical adaptation and/or by means of integrated molecular and cellular responses. To face the environmental challenge in the form of various abiotic stresses, perception of stress signals and their transduction is a very crucial step for switching on adaptive responses to ensure the survival of plants. Recent studies have revealed that understanding signal perception and its transduction is crucial for engineering stress tolerance in crop plants.

1.3 Abiotic Stress Signaling Pathways in Plants

In nature, tolerance and survival of plants are achieved by their capacity to make their responses flexible to environmental cues. In turn, the plant stress response flexibility is governed by the signaling pathways, interwoven at cellular and molecular levels [5]. In fact, the perception of abiotic stress initiates the signals that trigger downstream signaling processes and transcription controls and notify parallel pathways [1, 6]. In the signal transduction pathway, as a first step, perception of the signal is performed by receptors/sensors such as phytochromes, histidine kinases, receptor-like kinases, G-protein-coupled receptors, hormones). Second, the generation of secondary signaling molecules such as inositol phosphatase, reactive oxygen species (ROS), and abscisic acid (ABA) is accomplished. Subsequently, the secondary molecule-mediated modulation of intracellular Ca2+