PMID:1673017
| Citation |
Kumamoto, CA (1991) Molecular chaperones and protein translocation across the Escherichia coli inner membrane. Mol. Microbiol. 5:19-22 |
|---|---|
| Abstract |
Proteins that are able to translocate across biological membranes assume a loosely folded structure. In this review it is suggested that the loosely folded structure, referred to here as the 'pre-folded conformation', is a particular structure that interacts favourably with components of the export apparatus. Two soluble factors, SecB and GroEL, have been implicated in maintenance of the pre-folded conformation and have been termed 'molecular chaperones'. Results suggest that SecB may be a chaperone that is specialized for binding to exported protein precursors, while GroEL may be a general folding modulator that binds to many intracellular proteins. |
| Links | |
| Keywords |
Bacterial Proteins/metabolism; Biological Transport; Cell Membrane/metabolism; Chaperonin 60; Escherichia coli/metabolism; Heat-Shock Proteins/metabolism; Protein Conformation; Protein Precursors/metabolism |
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