The universally conserved GroE (Hsp60) chaperonins

This report will discuss the following topics: the groE operon; the GroE proteins; evolutionary conservation of groES and groEL; function of the groE genes in bacteriophage morphogenesis; function of the GroE proteins in E. coli physiology; defining substrates of GroE chaperonins; a model for GroES-...

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Bibliographic Details
Published in:	Annual review of microbiology Vol. 45; no. 1; pp. 301 - 325
Main Authors:	ZEILSTRA-RYALLS, J, FAYET, O, GEORGOPOULOS, C
Format:	Journal Article
Language:	English
Published:	Palo Alto, CA Annual Reviews 01-01-1991
Subjects:	Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Biological and medical sciences Biological Evolution Chaperonin 10 Chaperonin 60 Coliphages - growth & development Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Heat-Shock Proteins - chemistry Heat-Shock Proteins - genetics Microbiology Miscellaneous Molecular Sequence Data Operon phage lambda phage T4 T-Phages - growth & development Operon Escherichia coli Molecular interaction Review Gene expression Structure function relationship Biological activity Virus Molecular evolution Regulation(control) Gene Heat shock protein Bacteria Aminoacid sequence Enterobacteriaceae Phage
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Summary:	This report will discuss the following topics: the groE operon; the GroE proteins; evolutionary conservation of groES and groEL; function of the groE genes in bacteriophage morphogenesis; function of the GroE proteins in E. coli physiology; defining substrates of GroE chaperonins; a model for GroES-GroEL action.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 ObjectType-Feature-3 ObjectType-Review-1
ISSN:	0066-4227 1545-3251
DOI:	10.1146/annurev.mi.45.100191.001505