The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.
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.
Departments of Stomatology and Microbiology, University of California, San Francisco, 513 Parnassus Avenue, CA 94143, USA. sbehren@Uni-Molgen.gwdg.de
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Behrens
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Maier
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de Cock
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Schmid
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Gross
D001426:Bacterial Proteins / Q000378:metabolism; D002352:Carrier Proteins; D002950:Citrate (si)-Synthase / Q000737:chemistry / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics*; D029968:Escherichia coli Proteins; D005838:Genotype; D007700:Kinetics; D018832:Molecular Chaperones / Q000378:metabolism; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019696:Peptidylprolyl Isomerase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D010957:Plasmids; D017510:Protein Folding; D006163:Ribonuclease T1 / Q000737:chemistry / Q000378:metabolism; D017384:Sequence Deletion
D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D002950:Citrate (si)-Synthase; D006163:Ribonuclease T1; C490900:SurA protein, E coli; C098640:periplasmic peptidylprolyl cis-trans isomerase; D019696:Peptidylprolyl Isomerase; C000606851:parvA protein, E coli