Springer Biomedical and Life Sciences eBooks 2017 English+International

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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

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

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

This book focuses on a topical and timely aspect of prokaryotic biology - the biology of prokaryotic multiple chaperonins. Chaperonins are a class of molecular chaperones, the proteins that assist folding of other proteins in the cell. The book begins with an introductory chapter on the structural and functional aspects of chaperonins, followed by an outline on different mechanisms of their regulation. Subsequently, the book provides a comprehensive overview on how the multiple-chaperonins have embraced biological requirements in different classes of microbes, discussing their functional diversity, evolutionary paths and the latest advances in the field. It brings together leading experts from across the globe in offering a detailed account of the structural, biochemical, functional and phylogenetic characteristics of microbial chaperonins for students, researchers and teachers working in the area of microbiology/ biophysics/ parasitology - more specifically, in protein folding pathways. .