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Protein folding in Escherichia coli: the chaperonin GroE and its substrates.
- Source :
-
Research in microbiology [Res Microbiol] 2009 May; Vol. 160 (4), pp. 267-77. Date of Electronic Publication: 2009 Apr 23. - Publication Year :
- 2009
-
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.
- Subjects :
- Escherichia coli chemistry
Escherichia coli Proteins physiology
HSP70 Heat-Shock Proteins chemistry
HSP70 Heat-Shock Proteins physiology
Heat-Shock Proteins physiology
Stress, Physiological
Substrate Specificity
Escherichia coli metabolism
Escherichia coli Proteins chemistry
Heat-Shock Proteins chemistry
Protein Folding
Subjects
Details
- Language :
- English
- ISSN :
- 1769-7123
- Volume :
- 160
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Research in microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 19393741
- Full Text :
- https://doi.org/10.1016/j.resmic.2009.04.002