Jacquot Oxidative Stress and Redox Regulation in Plants

1. Auflage 2009
ISBN: 978-0-12-378623-4
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 52, 350 Seiten

Reihe: Advances in Botanical Research

The field of redox is rapidly changing, specifically in relation to plants where redox reactions are exacerbated compared to non-photosynthetic organisms. The development of proteomics has allowed the identification of hundreds of molecular targets of these systems, and the recent discovery of glutaredoxin's ability to bind iron sulfur centers (ISCs) and to participate in ISC assembly in other apoproteins has provided many new insights. This volume presents new research on oxidative stress in plants, ranging from the production of reactive oxygen species or reactive nitrogen species, to their accumulation, their involvement in signal transduction, and their degradation, while also covering the links among oxidative stress and biotic and abiotic stresses. - Cutting-edge reviews written from a broad range of scientific perspectives - For over 40 years, series has enjoyed a reputation for excellence - Contributors internationally recognized authorities in their respective fields

Autoren/Hrsg.

Jacquot, Jean-Pierre

Inhaltsverzeichnis

1;Front Cover;1
2;Advances in Botanical Research: Oxidative stress and redox regulation in plants;4
3;Copyright;5
4;Contents;6
5;Contributors to Volume 52;12
6;Preface;18
7;Contents of Volumes 35–51;22
8;Chapter 1: Oxidation of Proteins in Plants-Mechanisms and Consequences;38
8.1;I Introduction;39
8.2;II The Formation of ROS and RNS;39
8.3;III Mechanisms of Oxidation of Proteins;42
8.4;IV Methods for Measuring Protein Oxidation;44
8.5;V Which Proteins, Which Oxidations?;48
8.6;VI Does Protein Oxidation Mean Protein Dysfunction?;51
8.7;VII Removal and Processing of Oxidized Proteins;53
8.8;VIII The Cost of Protein Oxidation;54
8.9;IX Summary;55
8.10;References;55
9;Chapter 2: Reactive Oxygen Species: Regulation of Plant Growth and Development;62
9.1;I Introduction;63
9.2;II Redox Regulation;65
9.3;III Plant Hormones and ROS;67
9.4;IV Polarized Cell Growth and Development;74
9.5;Acknowledgment;78
9.6;References;78
10;Chapter 3: Ultraviolet-B Induced Changes in Gene Expression and Antioxidants in Plants;84
10.1;I Introduction;85
10.2;II UV-B Perception;86
10.3;III UV-B Induced Signal Transduction;88
10.4;IV Regulation of Gene Expression by UV-B;90
10.5;V Sources of ROS;93
10.6;VI Metabolism of ROS;103
10.7;VII Conclusion;110
10.8;References;111
11;Chapter 4: Roles of gamma-Glutamyl Transpeptidase and gamma-Glutamyl Cyclotransferase in Glutathione and Glutathione-Conjugat Metabolism in Plants;124
11.1;I Introduction;125
11.2;II Characteristics of GGTs;127
11.3;III Physiological Functions of GGT in Animals;127
11.4;IV Physiological Functions of GGTs in Plants;129
11.5;V Three-dimensional Structures of GGTs from Bacteria and Arabidopsis;135
11.6;VI GGT-like Proteins in other Plants than Arabidopsis;140
11.7;VII The Pathway for GSH Degradation in the Cytosol in Plants;141
11.8;VIII Differences in the GSH Degradation Pathways between Animals and Plants;143
11.9;IX Perspective;144
11.10;Acknowledgment;144
11.11;References;145
12;Chapter 5: The Redox State, a Referee of the Legume-Rhizobia Symbiotic Game;152
12.1;I Introduction;153
12.2;II Production of Reactive Oxygen Species During Legume–Rhizobia Symbiosis;153
12.3;III Involvement of Antioxidant Systems in•the Legume–Rhizobium •Symbiosis;160
12.4;IV Redox Control of NFS Under Environmental Stresses;170
12.5;V Conclusions and Perspectives;174
12.6;Acknowledgment;176
12.7;References;176
13;Chapter 6: Reactive Oxygen Species in Phanerochaete chrysosporium: Relationship Between Extracellular Oxidative and Intracellu Antioxidant Systems;190
13.1;I Extracellular Reactive Oxygen Species (ROS) Formation;191
13.2;II Intracellular ROS Formation;196
13.3;III How to Deal with Intracellular ROS?;201
13.4;IV Relationship Between Intracellular ROS and Lignin Degradation;213
13.5;References;215
14;Chapter 7: Physiological Impact of Thioredoxin- and Glutaredoxin-Mediated Redox Regulation in Cyanobacteria;224
14.1;I Introduction: The Redox-Balancing System in Cyanobacteria;225
14.2;II Synchronization Between Redox Equilibrium and Photosynthesis;226
14.3;iii. Physiological Phenomena Controlled by Redox: Gene Expression;228
14.4;IV Physiological Phenomena Controlled by Redox: Protein Synthesis;229
14.5;V The Proteomic Approach Reveals a•Variety of T&lc;rx Target Proteins;231
14.6;VI Perspectives;237
14.7;Acknowledgment;238
14.8;References;238
15;Chapter 8: Use of Transgenic Plants to Uncover Strategies for Maintenance of Redox Homeostasis During Photosynthesis;244
15.1;I Introduction: Studying Control of Redox Networks;246
15.2;II Balancing Redox Networks Within PET;250
15.3;III Buffering of Redox Poise by Coordinated and Compensatory Pathways;256
15.4;IV Changes in Redox State are Translated into Signaling Cascades to Adjust•Metabolism;265
15.5;V Conclusions;272
15.6;Acknowledgment;276
15.7;References;276
16;Chapter 9: Redundancy and Crosstalk Within the Thioredoxin and Glutathione Pathways: A New Development in Plants;290
16.1;I Introduction;291
16.2;II NTS and NGS Overlap in Bacteria and•Yeast;292
16.3;III Overlaps and Crosstalks in Animals;295
16.4;IV Crosstalks in Plants;296
16.5;V Conclusions;305
16.6;Acknowledgment;306
16.7;References;306
17;Chapter 10: Protein Import in Chloroplasts: An Emerging
Regulatory Role for Redox;314
17.1;I Introduction;315
17.2;II Pathways of Protein Import in Chloroplasts;317
17.3;III Molecular Machineries Involved in Protein Translocation Through the Chloroplast Envelope Membranes: The General Import Pathway;321
17.4;IV Structure-Function Relations of TOC and TIC Components: Potential for Redox Regulation;323
17.5;V Regulation of Chloroplast Protein Import by Metabolic and Environmental Redox State;343
17.6;VI Further Possible Redox Targets in Chloroplast Protein Import;349
17.7;Acknowledgment;355
17.8;References;355
18;Chapter 11: Glutaredoxins in Development and Stress Responses of Plants;370
18.1;I Introduction;372
18.2;II Evolutionary Implications of Land Plant-Specific CC-Type GRXs;373
18.3;III ROXY1 and ROXY2, Two CC-Type GRX Genes, Regulate Flower Development;374
18.4;IV CC-Type GRXs; with A Conserved C-Terminus Can Modify the Same Target Proteins If Expressed Properly;376
18.5;V ROXY1 Interacts with TGA Transcription Factors in the Nucleus;377
18.6;VI Genetic Interaction of ROXY1 with TGA Genes;378
18.7;VII CC-Type GRXs and Disease Resistance;380
18.8;VIII Comparisons of Signaling Mechanisms Involved in Disease Resistance and Flower Development;381
18.9;IX CPYC and CGFS GRXs Act in Iron–Sulfur Cluster Formation and Arsenic Resistance;384
18.10;X GSH-Associated Developmental Processes;387
18.11;XI Oxidative Stress Responses;389
18.12;XII Identification of GRX Targets;391
18.13;XIII Crosstalks Between GRXs and TRXs;392
18.14;XIV Concluding Remarks;392
18.15;References;393
19;Chapter 12: Glutathionylation in Photosynthetic Organisms;400
19.1;I Introduction;401
19.2;II Glutathionylation Reactions;404
19.3;III Deglutathionylation Reactions;409
19.4;IV Methods for Identification and Analysis of Glutathionylated Proteins;414
19.5;V Glutathionylation in Nonphotosynthetic Organisms;420
19.6;VI Glutathionylation in Photosynthetic Organisms;422
19.7;VII Multiple Interconnections;426
19.8;Acknowledgment;427
19.9;References;427
20;Chapter 13: Glutaredoxin: The Missing Link Between Thiol-Disulfide
Oxidoreductases and Iron Sulfur Enzymes;442
20.1;I Introduction;443
20.2;II Iron-Containing Enzymes;444
20.3;III Thiol-Disulfide Oxidoreductases;449
20.4;IV Early Experiments Suggesting a Link Between Iron Sulfur Enzymes and Redoxins;458
20.5;V Glutaredoxins Bind ISCs;460
20.6;VI Glutaredoxins Help Transfer ISCs in Apoproteins;463
20.7;VII Concluding Remarks;464
20.8;References;464
21;Chapter 14: Oxidative Stress and Thiol-Based Antioxidants in Cereal Seeds;474
21.1;I Introduction;475
21.2;II The Life Cycle of Cereal Seeds: Development and Germination;476
21.3;III Developing and Germinating Seeds Suffer Oxidative Stress;479
21.4;IV Seed Redox Systems;481
21.5;V Concluding Remarks and Future Prospects;490
21.6;Acknowledgment;491
21.7;References;491
22;Chapter 15: Molecular Recognition in NADPH-Dependent Plant Thioredoxin Systems-Catalytic Mechanisms, Structural Snapshots and Target Identifications;498
22.1;I Introduction;499
22.2;II Components of NADPH-Dependent Trx Systems in Plants;501
22.3;III Structural Snapshots and Catalytic Mechanisms;506
22.4;IV Identification of Trx Targets by Proteomics Approaches;519
22.5;V Summary and Perspectives;524
22.6;Acknowledgment;524
22.7;References;524
23;Color Plates;560

Leseproben

Chapter 1 Oxidation of Proteins in Plants—Mechanisms and Consequences

Lee J. Sweetlove*1 (email: [e-mail]) and Ian M. Møller†

*Department of Plant Sciences, University of Oxford, South Parks Road, Oxford OX1 3RB, United Kingdom

†Department of Genetics and Biotechnology, Faculty of Agricultural Sciences, Aarhus University, Forsøgsvej 1, DK-4200 Slagelse, Denmark

1Corresponding author:

Abstract

The production of reactive oxygen and reactive nitrogen species in plant cells can lead to a variety of modifications of proteins through oxidation of amino acid side groups. The widespread occurrence of such modifications is becoming appreciated as new proteomic approaches allow their systematic identification. Oxidized amino acid residues can be identified directly by mass spectrometry if the modification is stable, but it is more common to covalently tag the oxidized group by reaction with a marker molecule. The marker molecule generally allows visualization through immuno-detection and isolation of modified proteins by affinity purification. Although there are several technical caveats with such approaches, they have been useful in documenting the extent of oxidative modification of proteins and have highlighted a number of proteins where oxidative modification is critical for protein function. A view that such modifications could have signalling ramifications is emerging. However, in many cases there is a lack of information as to the effect of oxidation on protein activity or function. Severe protein oxidation is costly to the cell since oxidatively damaged proteins need to be degraded by specific proteases or damaged cellular components recycled via the autophagy pathway. Avoiding this cost is clearly advantageous, and it has been proposed that proteins may have an over-representation of easily oxidizable amino acids on their surface to act as decoy or sacrificial residues, thus preventing or postponing oxidation of residues more important for the function of the protein.

I. Introduction

Oxidative stress occurs when the rate of production of reactive oxygen (ROS) and/or reactive nitrogen species (RNS) is greater than the capacity of the cell's antioxidant defences to detoxify them. As a consequence, the extent to which ROS and RNS oxidize key cellular macromolecules is dramatically increased. Some of these oxidation events may prevent the normal functioning of the target macromolecules, and the resulting change in cellular homeostasis is referred to as oxidative stress. Along with lipids, proteins are the key class of macromolecules in the cell that can be oxidized in a way that contributes to cellular oxidative stress. The aim of this chapter is to review recent advances in our understanding of the process of protein oxidation. We will briefly introduce the production of ROS and RNS, summarize the main mechanisms by which proteins can be oxidized, before reviewing recent work providing an overview of the proteins that are targets of oxidation, and the importance of specific oxidation events in the regulation of cellular processes. We will also consider the cost of protein oxidation and describe our current understanding of the mechanisms by which oxidized proteins are processed and removed.

II. The Formation of ROS and RNS

The biochemistry of formation of ROS and RNS has been extensively reviewed and we do not wish to reproduce this exhaustive information here. Our aim in this section is to briefly outline the main points and provide the context for the rest of the chapter. For a more detailed account of the chemistry and biochemistry of ROS and RNS formation, the reader should consult Halliwell and Gutteridge's excellent textbook (Halliwell and Gutteridge, 2007). In addition, there are numerous relevant plant-specific reviews that we wholeheartedly recommend (Apel and Hirt, 2004, del Rio et al., 2006, Delledonne, 2005, Halliwell, 2006, Moller, 2001, Møller et al., 2007, Noctor and Foyer, 1998, Noctor et al., 2007 and Rinalducci et al., 2008).

ROS are produced either by partial, single-electron reduction of oxygen to generate superoxide, hydrogen peroxide and hydroxyl radicals or by alteration of oxygen electron spin states by photoactivation to generate singlet oxygen (Fig. 1). The latter happens exclusively in the chloroplast via a photosensitization reaction involving photosystem II. In the light, the chloroplast is also the main source of superoxide (Foyer and Noctor, 2003) as a result of ‘electron leakage’ from the photosynthetic electron transport chain. However, significant quantities of superoxide are also generated as a by-product of the mitochondrial electron transport chain (Foyer and Noctor, 2003 and Moller, 2001) and in the apoplast as a consequence of NADPH oxidase activity in response to biotic (Sagi and Fluhr, 2001) and abiotic (Achard et al., 2008) stresses. Superoxide will rapidly chemically dismutate to form hydrogen peroxide, a reaction that is accelerated manyfold by the presence of superoxide dismutases in most subcellular compartments. Hydrogen peroxide is also generated directly in very large quantities in peroxisomes as a by-product of photorespiratory metabolism and the ?-oxidation of fatty acids. In the presence of reduced transition metals, Fenton chemistry reduces hydrogen peroxide to the extremely reactive hydroxyl radical.

Fig. 1 Formation of the most important reactive oxygen species (A) and reactive nitrogen species (B).

Different ROS vary significantly in terms of their properties and reactivity; the order of reactivity being hydroxyl radical > superoxide > hydrogen peroxide. Their reactivity sets limits on how far different ROS can propagate from their site of production. The hydroxyl radical is so reactive that it will react more or less indiscriminately with the first molecule it encounters. In contrast, the relatively low reactivity of hydrogen peroxide means that it can accumulate to significant concentrations and can diffuse as far as 1 ?m from its site of production (Møller et al., 2007). Superoxide will travel a shorter distance (up to 30 nm) and moreover, as a charged species at cellular pH (pKa 4.8—Halliwell and Gutteridge, 2007), it is confined to the subcellular compartment in which it is produced. The superoxide formed by the NADPH oxidase outside the plasma membrane, where the pH is normally significantly lower than inside the cell, could be substantially protonated and may find it easier to enter the cell by crossing the plasma membrane as a neutral molecule.

Plants also produce RNS, particularly nitric oxide (NO•) and peroxynitrite (ONOO?). It remains unclear what is the most significant source of NO in plant cells. Efforts to uncover a canonical nitric oxide synthase, analogous to that found in mammals, have been beset with controversy (Zemojtel et al., 2006). A putative nitric oxide synthase in Arabidopsis (Guo and Crawford, 2005) was ultimately revealed to be incapable of NO synthesis from arginine and instead was established as a plastid-localized GTPase (Gas et al., 2009). This protein is still linked with NO• production (knockouts reduce NO• levels) but the mechanism is unclear. There are two other potential sources of NO• in plants: nitrate reductase and the mitochondrial electron transport chain under anoxia. Nitrate reductase can reduce nitrite to NO•. This could occur in vivo when the nitrite accumulates (the preferred substrate of nitrate reductase is, of course, nitrate) such as during anoxia when nitrite reductase is inhibited (Meyer et al., 2005). Anoxia is also a prerequisite for NO• production by mitochondria, allowing nitrite to serve as an alternative terminal electron acceptor in the electron transport chain. Because NO• inhibits complex IV of the respiratory chain, but not the alternative oxidase, NO• production has been proposed as a mechanism for controlling respiratory balance under low oxygen (Benamar et al., 2008 and Borisjuk et al., 2007). Whatever the mechanisms of NO• synthesis, there are reliable measurements demonstrating its presence in a range of plant tissues. Although NO• is a radical, its reactivity with proteins is limited. However, NO• does react extremely readily with superoxide to form peroxynitrite and this anion is more significant in terms of protein oxidation.

III. Mechanisms of Oxidation of Proteins

The following protein amino acids contain side groups that can be oxidized by different ROS and RNS leading to stable covalent modifications: Cys, Met, His, Arg, Lys, Pro, Tyr and Trp. The reactions are summarized in Fig. 2. Most of these reactions are essentially irreversible, although in the specific case of oxidation of thiols, enzyme-catalyzed re-reduction is possible (Bechtold et al., 2004 and Rouhier et al., 2006). Considering only the oxidation by ROS, most of the oxidation reactions shown in Fig. 2 are found to be only triggered by the highly reactive hydroxyl radical or singlet oxygen. This means that such oxidation events are only likely to occur in proteins that are localized extremely close to the site of production of these radicals.

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