title: Protein folding in Escherichia coli: the chaperonin GroE and its substrates.
abstract: A brief summary of the role of DnaK and GroE chaperones in protein folding precedes a discussion of the role of GroE in Escherichia coli. We consider its obligate substrates, the 8 that are both obligate and essential, and the prospects for constructing a mutant that could survive without it. Structural features of GroE-dependent polypeptides are also considered.
authors.affiliation: Institute of Cell Biology, University of Edinburgh, Kings Buildings, Edinburgh EH93JR, Scotland, United Kingdom. m.masters@ed.ac.uk
authors.forename: Millicent
authors.initials: M
authors.lastname: Masters
authors.forename: Garry
authors.initials: G
authors.lastname: Blakely
authors.forename: Andrew
authors.initials: A
authors.lastname: Coulson
authors.forename: Neil
authors.initials: N
authors.lastname: McLennan
authors.forename: Vollodymyr
authors.initials: V
authors.lastname: Yerko
authors.forename: John
authors.initials: J
authors.lastname: Acord
mesh_terms: D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000502:physiology; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000502:physiology; D017510:Protein Folding; D013312:Stress, Physiological; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; C028715:GroE protein, E coli; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C063842:dnaK protein, E coli