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PMID: 3049077 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

ProOmpA spontaneously folds in a membrane assembly competent state which trigger factor stabilizes.

The EMBO journal ·Vol. 7 ·No. 6 ·1988-06-00 ·Pages 1831-5

Crooke E, Brundage L, Rice M, Wickner W

Abstract

The precursor protein proOmpA can translocate across purified Escherichia coli inner membrane vesicles in the absence of any other soluble proteins. ProOmpA, purified 2000-fold in the presence of 8 M urea, is competent for translocation following rapid renaturation via dilution. ATP, the transmembrane electrochemical potential, and functional secY protein are essential for the translocation of proOmpA renatured by dilution. The kinetics of its translocation and the level of translocation at each concentration of ATP are indistinguishable from that of proOmpA renatured by dialysis with trigger factor. After dilution, the proOmpA rapidly loses its competence for membrane assembly. However, this competence is stabilized by trigger factor. Assembly-competent proOmpA is in a protease-sensitive conformation, whereas proOmpA which has lost this competence is more resistant to degradation. This suggests that the primary role for trigger factor in in vitro protein translocation is to maintain precursor proteins in a translocation-competent conformation. We propose that a properly folded precursor protein and ATP are the only soluble components which are essential for bacterial protein translocation.

MeSH Terms
Adenosine Triphosphate/metabolism Bacterial Outer Membrane Proteins/metabolism Bacterial Proteins/metabolism Biological Transport Cell Membrane/metabolism Escherichia coli/metabolism Protein Conformation Protein Precursors/metabolism Protein Processing, Post-Translational
Chemicals
Bacterial Outer Membrane Proteins Bacterial Proteins Protein Precursors Adenosine Triphosphate
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Crooke E
Molecular Biology Institute, University of California, Los Angeles 900524-1570.
Brundage L
Rice M
Wickner W
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32 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1988-06-00
Pages
1831-5
Language
English
Region
England
NLM ID
8208664
PMCID
PMC457175
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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