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PMID: 2872675 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 83 ·No. 12 ·1986-06-00 ·Pages 4219-22

Geller BL, Movva NR, Wickner W

Abstract

Pro-OmpA is processed to OmpA by isolated inverted plasma membrane vesicles from Escherichia coli. In the presence of ATP and a membrane potential, 58% (+/- 13%) of the OmpA is sequestered in the vesicles. We sought to determine which of these two metabolic energy sources is used for protein translocation. The plasma membrane F1F0-ATPase is the central enzyme that interconverts the energy of membrane electrochemical potential and ATP. To separate the effects of these two forms of energy in vitro, the ATPase was inactivated, either by "stripping" the F1 from the membranes with low salt and EDTA or by using membrane vesicles derived from a strain without the atp operon. In each case, optimal translocation and processing of pro-OmpA required both a membrane potential and ATP. We conclude that ATP and membrane potential are separate requirements for bacterial protein export.

MeSH Terms
Adenosine Triphosphate/physiology Bacterial Outer Membrane Proteins/metabolism Biological Transport Cell Compartmentation Cell Membrane/physiology Escherichia coli Membrane Potentials NAD/metabolism Protein Precursors/metabolism Proton-Translocating ATPases/metabolism
Chemicals
Bacterial Outer Membrane Proteins Protein Precursors NAD Adenosine Triphosphate Proton-Translocating ATPases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Geller B L
Movva N R
Wickner W
References (19)
19 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.83.12.4219
Published
1986-06-00
Pages
4219-22
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC323703
Subset
IM
Grants
NHLBI NIH HHS · HL 07386 · United States
External Links
PubMed source DOI: 10.1073/pnas.83.12.4219 PMC Full Text View journal details
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