PMID:11123702
| Citation |
Arié, JP, Sassoon, N and Betton, JM (2001) Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 39:199-210 |
|---|---|
| Abstract |
The nature of molecular chaperones in the periplasm of Escherichia coli that assist newly translocated proteins to reach their native state has remained poorly defined. Here, we show that FkpA, a heat shock periplasmic peptidyl-prolyl cis/trans isomerase (PPIase), suppresses the formation of inclusion bodies from a defective-folding variant of the maltose-binding protein, MalE31. This chaperone-like activity of FkpA, which is independent of its PPIase activity, requires a full-length structure of the protein. In vitro, FkpA does not catalyse a slow rate-limiting step in the refolding of MalE31, but prevents its aggregation at stoichiometric amounts and promotes the reactivation of denaturated citrate synthase. We propose that FkpA functions as a chaperone for envelope proteins in the bacterial periplasm. |
| Links | |
| Keywords |
ATP-Binding Cassette Transporters; Binding Sites/genetics; Carrier Proteins/metabolism; Circular Dichroism; Citrate (si)-Synthase/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Heat-Shock Proteins/metabolism; Heat-Shock Response; Immunophilins/genetics; Immunophilins/metabolism; Inclusion Bodies; Maltose-Binding Proteins; Membrane Proteins/genetics; Membrane Proteins/metabolism; Monosaccharide Transport Proteins; Peptidylprolyl Isomerase/metabolism; Periplasm/metabolism; Periplasmic Binding Proteins; Protein Folding; Protein Structure, Secondary; Protein Transport; Sequence Deletion |
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