Annual Plant Reviews, Protein-Protein Interactions in Plant Biology (Annual Plant Reviews)

Contents......Page 12
1.1 Introduction......Page 18
1.2 Description of the chloroplastic and cytosolic systems in eukaryotic plants......Page 19
1.3 Mechanism of thioredoxin catalysis and consequences......Page 20
1.4.1 Thioredoxin reductases......Page 23
1.4.2 Ferredoxin–thioredoxin reductase (FTR)......Page 25
1.4.3 Target enzymes......Page 28
1.4.4 Fructose-1,6-bisphosphatase......Page 33
1.4.5 Interaction of plant thioredoxins with yeast targets......Page 36
1.5 New approaches for the characterization of thioredoxin targets......Page 37
References......Page 40
2.2 Structure of Rubisco and the activase......Page 47
2.2.3 Member of the AAA[sup(+)] protein super-family......Page 48
2.3 Activities and mechanism of activase......Page 50
2.3.1 Dissociation of Rubisco–sugar phosphate complexes......Page 52
2.3.2 Hydrolysis of ATP and inhibition by ADP......Page 53
2.3.3 Oligomer formation and its relationship to activase activity......Page 54
2.3.4 Key residues identified in activase and its AAA[sup(+)] domains......Page 55
2.3.5 Specificity of interaction with Rubisco: identification of a Rubisco binding site......Page 56
2.3.6 Conformational changes in Rubisco and a model for the activase mechanism......Page 57
2.4.1 ADP/ATP regulation and redox regulation by thioredoxin f......Page 59
2.4.2 A role in the temperature response of photosynthesis......Page 61
2.5 Future perspectives......Page 63
References......Page 64
3.2 Structure and biochemical characterization of 14-3-3 proteins......Page 70
3.3 Plant 14-3-3 protein families and organization......Page 73
3.4 Mode of action of 14-3-3 proteins......Page 76
3.5 14-3-3 proteins and the regulation of metabolic enzymes......Page 77
3.6 14-3-3 proteins and the regulation of non-metabolic enzymes......Page 82
3.7 Isoform preference for 14-3-3 target proteins......Page 84
3.8 Localization of plant 14-3-3s......Page 85
3.9 Potential 14-3-3 binding partners in plants......Page 88
References......Page 89
4.1 Introduction......Page 94
4.2 The functions of PIs......Page 96
4.3 The classification of PIs......Page 98
4.4.1 Serpins......Page 101
4.4.2 The Kunitz family......Page 105
4.4.3 The Bowman–Birk family......Page 106
4.4.4 The PI 1 family......Page 108
4.4.5 The PI 2 family......Page 109
4.4.6 The squash family inhibitors......Page 113
4.4.7 The mustard seed inhibitors......Page 114
4.4.8 The cereal trypsin/α-amylase inhibitor family......Page 115
4.4.9 Other serine proteinase inhibitors......Page 116
4.5.1 The cystatins......Page 117
4.5.2 The Kunitz cysteine PIs......Page 118
4.5.4 Miscellaneous cysteine PIs......Page 120
4.6 Proteinaceous inhibitors of metalloproteinases......Page 121
4.8 Concluding remarks......Page 122
References......Page 123
5.1 Introduction......Page 137
5.2.1 Phosphoribulokinase–glyceraldehyde-3-phosphate dehydrogenase......Page 139
5.2.2 Phosphoglycerate kinase–glyceraldehyde 3-phosphate dehydrogenase......Page 144
5.2.3 Phosphoribose isomerase–phosphoribulokinase–ribulose-1,5-bisphosphate carboxylase-oxygenase......Page 145
5.2.4 Phosphoribose isomerase–phosphoribulokinase–ribulose-1,5-bisphosphate carboxylase/oxygenase–phosphoglyceratekinase–glyceraldehyde-3-phosphate.........Page 146
5.3 Supramolecular complexes involved in fatty acid metabolism......Page 147
5.3.1 Acetyl CoA carboxylases......Page 148
5.3.2 Fatty acid synthases......Page 150
5.4 Kinetic aspects of multienzyme complexes......Page 158
5.5 Conclusion......Page 160
References......Page 161
6.2 Physical properties of the proteosome......Page 168
6.2.1 The 20S core......Page 170
6.2.2 The 19S regulatory complex......Page 173
6.2.3 Mechanisms to target identification—ubiquitylation......Page 174
6.2.4 Recognition sites......Page 178
6.2.5 Regulation of substrates by phosphorylation......Page 179
6.2.7 Ornithine decarboxylase......Page 180
6.3.1 Biotic stress......Page 181
6.3.2 Abiotic stress......Page 182
6.3.3 Growth and differentiation......Page 183
6.4.1 Physical properties......Page 185
6.4.2 Subunits and active sites......Page 186
6.5 Lon proteases......Page 187
6.6 Conclusions......Page 188
References......Page 189
7.1 Chaperonins......Page 198
7.2.1 Bacterial chaperonins......Page 199
7.2.2 The chloroplast chaperonins......Page 201
7.2.3 Mitochondrial chaperonins......Page 210
7.3 Type II chaperonins......Page 212
7.4 Concluding remarks......Page 213
References......Page 214
8.1 Introduction......Page 221
8.2.1 RLKs......Page 222
8.2.2 Receptor histidine kinases......Page 233
8.3.1 Expression patterns......Page 238
8.3.2 Transcriptional and post-transcriptional regulation......Page 239
8.3.3 Self-incompatibility......Page 240
8.4 Toward understanding receptor histidine kinase function......Page 241
8.5 Identification of ligands and downstream elements......Page 242
8.5.1 CLAVATA and meristem fate......Page 243
8.5.2 Pollen self-incompatibility......Page 245
8.6 Comparison of similar proteins in animal cells......Page 246
References......Page 248
9.1 Introduction......Page 255
9.2.2 Diversity of MAPK pathways......Page 256
9.2.4 MAPK complexes and scaffolds......Page 260
9.2.5 Plant MAPK pathways......Page 261
9.3 Cyclin-dependent protein kinases: the central regulators of cell division......Page 264
9.3.1 Cyclins: regulatory subunits of CDKs......Page 266
9.3.2 Regulation of CDK activity by phosphorylation......Page 267
9.3.3 CDK inhibitors......Page 269
References......Page 271
10.1 Introduction......Page 274
10.2 Plant DNA-binding transcription factors......Page 275
10.2.1 bZIP proteins......Page 276
10.2.3 bHLH proteins......Page 278
10.2.4 Auxin response factors......Page 279
10.2.5 AP2 domain proteins......Page 280
10.3.1 Regulation of anthocyanin biosynthesis and trichrome development......Page 281
10.3.2 Abscisic acid-regulated gene expression......Page 283
10.3.3 Regulation of storage protein gene transcription......Page 285
10.3.4 Regulation of flower development......Page 286
10.4.1 Light-regulated gene transcription......Page 288
10.4.2 Systemic acquired resistance signal induced transcription......Page 291
10.5 Extensive protein interactions leading to the assembly of transcriptional initiation complexes......Page 292
References......Page 294
11.1 Introduction......Page 302
11.2 Calmodulin sequences and structures......Page 303
11.2.1 EF-hands, Ca[sup(2+)]-binding and intermolecular tuning by target proteins......Page 305
11.2.2 Hydrophobic interaction: Met puddles and conserved Phe residues......Page 308
11.2.3 The central helix: a flexible linker domain......Page 311
11.2.4 Additional structure-function relationships of CaM......Page 312
11.2.5 CaM isoforms in plants: what are the limits of the CaM gene family?......Page 313
11.3 Structures of Ca[sup(2+)]/CaM–target peptide complexes......Page 316
11.3.1 Structures of CaM-binding domains......Page 318
11.3.2 Energetics of target peptide binding by CaM......Page 321
11.3.3 Mechanisms of CaM-mediated activation......Page 322
11.4 Prospects for monitoring calmodulin function in vivo......Page 323
References......Page 326
B......Page 332
C......Page 333
D......Page 334
F......Page 335
K......Page 336
M......Page 337
P......Page 338
R......Page 339
S......Page 340
T......Page 341
Z......Page 342