000798394 000__ 04572cam\a2200529Ia\4500 000798394 001__ 798394 000798394 005__ 20230306143522.0 000798394 006__ m\\\\\o\\d\\\\\\\\ 000798394 007__ cr\un\nnnunnun 000798394 008__ 170905s2017\\\\si\\\\\\ob\\\\000\0\eng\d 000798394 019__ $$a1002418592$$a1003096881 000798394 020__ $$a9789811046513$$q(electronic book) 000798394 020__ $$a9811046514$$q(electronic book) 000798394 020__ $$z9789811046506 000798394 020__ $$z9811046506 000798394 035__ $$aSP(OCoLC)on1002897944 000798394 035__ $$aSP(OCoLC)1002897944$$z(OCoLC)1002418592$$z(OCoLC)1003096881 000798394 040__ $$aYDX$$beng$$cYDX$$dN$T$$dEBLCP$$dGW5XE$$dN$T$$dUAB 000798394 049__ $$aISEA 000798394 050_4 $$aQP552.M64 000798394 08204 $$a572/.6$$223 000798394 08204 $$a571.4 000798394 24500 $$aProkaryotic chaperonins :$$bmultiple copies and multitude functions /$$cC.M. Santosh Kumar, Shekhar C. Mande, editors. 000798394 260__ $$aSingapore :$$bSpringer,$$c2017. 000798394 300__ $$a1 online resource. 000798394 336__ $$atext$$btxt$$2rdacontent 000798394 337__ $$acomputer$$bc$$2rdamedia 000798394 338__ $$aonline resource$$bcr$$2rdacarrier 000798394 4901_ $$aHeat shock proteins,$$x1877-1246 ;$$vv. 11 000798394 504__ $$aIncludes bibliographical references. 000798394 5050_ $$aPreface; 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 000798394 5058_ $$a2.2.2 The Alternative Sigma Factor E2.2.3 The Alternative Sigma Factor H; 2.3 Regulation of the Heat Shock Response by Transcriptional Repressors; 2.3.1 The HrcA Repressor; 2.3.2 The CtsR Repressor; 2.3.3 The RheA Repressor; 2.3.4 The HspR Repressor; 2.4 Regulation of the Heat Shock Response by RNA Thermosensors; 2.5 Regulation of the Heat Shock Response by DNA Thermosensors; 2.5.1 DNA Supercoiling; 2.5.2 Promoter Curvature; 2.5.3 Nucleoid-Associated Proteins; References; Part II: Multiple Chaperonins of Bacterial System 000798394 5058_ $$aChapter 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 000798394 5058_ $$aChapter 4: Dynamic Interplay of the Myxobacterial Chaperonins4.1 Introduction; 4.2 Composition of the groEL and groES Genes in Myxobacteria; 4.3 Divergent Functions of the Two groEL Genes in M. xanthus DK1622; 4.4 Molecular Evolution of groEL1 and groEL2 for Functional Divergence; 4.5 Both GroELs Require GroES for Their Functions; 4.6 Synergic Expressions of the Single groES and the Double groELs; 4.7 Conclusion; References; Chapter 5: Functional Diversity in Mycobacterial Chaperonins: The Generalists and the Specialists; 5.1 Introduction 000798394 5058_ $$a5.2 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 000798394 506__ $$aAccess limited to authorized users. 000798394 588__ $$aDescription based on print version record. 000798394 650_0 $$aMolecular chaperones. 000798394 650_0 $$aProkaryotes. 000798394 7001_ $$aKumar, C. M. Santosh. 000798394 7001_ $$aMande, Shekhar C. 000798394 77608 $$iPrint version:$$z9789811046506$$z9811046506$$w(OCoLC)981117935 000798394 830_0 $$aHeat shock proteins (Series) ;$$vv. 11. 000798394 852__ $$bebk 000798394 85640 $$3SpringerLink$$uhttps://univsouthin.idm.oclc.org/login?url=http://link.springer.com/10.1007/978-981-10-4651-3$$zOnline Access$$91397441.1 000798394 909CO $$ooai:library.usi.edu:798394$$pGLOBAL_SET 000798394 980__ $$aEBOOK 000798394 980__ $$aBIB 000798394 982__ $$aEbook 000798394 983__ $$aOnline 000798394 994__ $$a92$$bISE