PMID:11226178
| Citation |
Behrens, S, Maier, R, de Cock, H, Schmid, FX and Gross, CA (2001) The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 20:285-94 |
|---|---|
| Abstract |
The Escherichia coli periplasmic peptidyl-prolyl isomerase (PPIase) SurA is involved in the maturation of outer membrane porins. SurA consists of a substantial N-terminal region, two iterative parvulin-like domains and a C-terminal tail. Here we show that a variant of SurA lacking both parvulin-like domains exhibits a PPIase-independent chaperone-like activity in vitro and almost completely complements the in vivo function of intact SurA. SurA interacts preferentially (>50-fold) with in vitro synthesized porins over other similarly sized proteins, leading us to suggest that the chaperone-like function of SurA preferentially facilitates maturation of outer membrane proteins. |
| Links |
PubMed PMC140197 Online version:10.1093/emboj/20.1.285 |
| Keywords |
Bacterial Proteins/metabolism; Carrier Proteins; Citrate (si)-Synthase/chemistry; Citrate (si)-Synthase/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Genotype; Kinetics; Molecular Chaperones/metabolism; Peptidylprolyl Isomerase/chemistry; Peptidylprolyl Isomerase/genetics; Peptidylprolyl Isomerase/metabolism; Plasmids; Protein Folding; Ribonuclease T1/chemistry; Ribonuclease T1/metabolism; Sequence Deletion |
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