Protein folding in Escherichia coli: the chaperonin GroE and its substrates.
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.
Masters
Millicent
M
Institute of Cell Biology, University of Edinburgh, Kings Buildings, Edinburgh EH93JR, Scotland, United Kingdom. m.masters@ed.ac.uk
Blakely
Garry
G
Coulson
Andrew
A
McLennan
Neil
N
Yerko
Vollodymyr
V
Acord
John
J
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
D029968:Escherichia coli Proteins; C028715:GroE protein, E coli; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C063842:dnaK protein, E coli