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Preface; Contents; About the Editors; Part I: Structure-Function of Chaperonins; Chapter 1: Structure, Function and Evolution of the Hsp60 Chaperonins; 1.1 Protein Folding: Early Days; 1.2 Structure and Function of GroEL and GroES; 1.3 Chaperonin Cycling; 1.4 The Evolutionary History of Chaperonins; 1.5 Chaperonin Interaction with Co-Chaperones and Chaperone Networks; 1.6 Chaperonin Substrates; References; Chapter 2: Regulation of the Heat Shock Response in Bacteria; 2.1 Introduction; 2.2 Regulation of the Heat Shock Response by Alternative Sigma Factors; 2.2.1 The Alternative Sigma Factor 32
2.2.2 The Alternative Sigma Factor E2.2.3 The Alternative Sigma Factor H; 2.3 Regulation of the Heat Shock Response by Transcriptional Repressors; 2.3.1 The HrcA Repressor; 2.3.2 The CtsR Repressor; 2.3.3 The RheA Repressor; 2.3.4 The HspR Repressor; 2.4 Regulation of the Heat Shock Response by RNA Thermosensors; 2.5 Regulation of the Heat Shock Response by DNA Thermosensors; 2.5.1 DNA Supercoiling; 2.5.2 Promoter Curvature; 2.5.3 Nucleoid-Associated Proteins; References; Part II: Multiple Chaperonins of Bacterial System
Chapter 3: Prokaryotic Multiple Chaperonins: The Mediators of Functional and Evolutionary Diversity3.1 Introduction; 3.2 Distribution of Multiple Chaperonins; 3.2.1 Functional Diversity Among the Chaperonins of Actinobacteria; 3.2.2 Unique Chaperonins in Firmicutes; 3.2.3 Functional Distribution Among the Chlamydial Chaperonins; 3.2.4 Rhizobial Chaperonins: The Aristocrats of Chaperonin Biology; 3.2.5 Multiple Chaperonins in Cyanobacteria: One Copy is Green!; 3.3 Why Multiple Chaperonins: Specific Examples; 3.4 A Note on Chaperonin Nomenclature; 3.5 Conclusions; References
Chapter 4: Dynamic Interplay of the Myxobacterial Chaperonins4.1 Introduction; 4.2 Composition of the groEL and groES Genes in Myxobacteria; 4.3 Divergent Functions of the Two groEL Genes in M. xanthus DK1622; 4.4 Molecular Evolution of groEL1 and groEL2 for Functional Divergence; 4.5 Both GroELs Require GroES for Their Functions; 4.6 Synergic Expressions of the Single groES and the Double groELs; 4.7 Conclusion; References; Chapter 5: Functional Diversity in Mycobacterial Chaperonins: The Generalists and the Specialists; 5.1 Introduction
5.2 Diversity in Mycobacterial Chaperonins: Sequence Features5.3 Structural Investigations on Mycobacterial Chaperonins; 5.3.1 Structural Studies on M. tuberculosis GroEL1; 5.3.2 Structural Studies on M. tuberculosis GroEL2; 5.4 Mycobacterial Chaperonins Are Functionally Diverse; 5.4.1 Mycobacterial Chaperonins Function as Antigens; 5.4.2 GroEL1 Works as a Specialized Chaperonin for Folding Pathogenic Proteins; 5.4.3 GroEL2 Functions as a Generalist Chaperonin; 5.5 Conclusions; References; Chapter 6: Multiple Chaperonins and Their Potential Roles in Rhizobia
2.2.2 The Alternative Sigma Factor E2.2.3 The Alternative Sigma Factor H; 2.3 Regulation of the Heat Shock Response by Transcriptional Repressors; 2.3.1 The HrcA Repressor; 2.3.2 The CtsR Repressor; 2.3.3 The RheA Repressor; 2.3.4 The HspR Repressor; 2.4 Regulation of the Heat Shock Response by RNA Thermosensors; 2.5 Regulation of the Heat Shock Response by DNA Thermosensors; 2.5.1 DNA Supercoiling; 2.5.2 Promoter Curvature; 2.5.3 Nucleoid-Associated Proteins; References; Part II: Multiple Chaperonins of Bacterial System
Chapter 3: Prokaryotic Multiple Chaperonins: The Mediators of Functional and Evolutionary Diversity3.1 Introduction; 3.2 Distribution of Multiple Chaperonins; 3.2.1 Functional Diversity Among the Chaperonins of Actinobacteria; 3.2.2 Unique Chaperonins in Firmicutes; 3.2.3 Functional Distribution Among the Chlamydial Chaperonins; 3.2.4 Rhizobial Chaperonins: The Aristocrats of Chaperonin Biology; 3.2.5 Multiple Chaperonins in Cyanobacteria: One Copy is Green!; 3.3 Why Multiple Chaperonins: Specific Examples; 3.4 A Note on Chaperonin Nomenclature; 3.5 Conclusions; References
Chapter 4: Dynamic Interplay of the Myxobacterial Chaperonins4.1 Introduction; 4.2 Composition of the groEL and groES Genes in Myxobacteria; 4.3 Divergent Functions of the Two groEL Genes in M. xanthus DK1622; 4.4 Molecular Evolution of groEL1 and groEL2 for Functional Divergence; 4.5 Both GroELs Require GroES for Their Functions; 4.6 Synergic Expressions of the Single groES and the Double groELs; 4.7 Conclusion; References; Chapter 5: Functional Diversity in Mycobacterial Chaperonins: The Generalists and the Specialists; 5.1 Introduction
5.2 Diversity in Mycobacterial Chaperonins: Sequence Features5.3 Structural Investigations on Mycobacterial Chaperonins; 5.3.1 Structural Studies on M. tuberculosis GroEL1; 5.3.2 Structural Studies on M. tuberculosis GroEL2; 5.4 Mycobacterial Chaperonins Are Functionally Diverse; 5.4.1 Mycobacterial Chaperonins Function as Antigens; 5.4.2 GroEL1 Works as a Specialized Chaperonin for Folding Pathogenic Proteins; 5.4.3 GroEL2 Functions as a Generalist Chaperonin; 5.5 Conclusions; References; Chapter 6: Multiple Chaperonins and Their Potential Roles in Rhizobia