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PMID: 1689050 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

In vitro trimerization of OmpF porin secreted by spheroplasts of Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 87 ·No. 2 ·1990-01-00 ·Pages 743-7

Sen K, Nikaido H

Abstract

It is not yet clear how bacterial outer membrane proteins reach their correct destination after they are secreted across the cytoplasmic membrane. We show here that porin OmpF is secreted into the medium as a water-soluble monomeric protein by spheroplasts of Escherichia coli. Furthermore, this monomeric porin is taken up by cell envelope preparations or purified lipopolysaccharides in the presence of 0.03% Triton X-100 and is converted correctly into the mature trimeric conformation. These results appear to reproduce a part of the physiological export and targeting steps of this protein.

MeSH Terms
Bacterial Outer Membrane Proteins/biosynthesis,isolation & purification,metabolism Electrophoresis, Polyacrylamide Gel Escherichia coli/metabolism Ion Channels/metabolism Macromolecular Substances Methionine/metabolism Molecular Weight Porins Spheroplasts/metabolism
Chemicals
Bacterial Outer Membrane Proteins Ion Channels Macromolecular Substances Porins Methionine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sen K
Department of Molecular and Cell Biology, University of California, Berkeley 94720.
Nikaido H
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24 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.87.2.743
Published
1990-01-00
Pages
743-7
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC53342
Subset
IM
Grants
NIAID NIH HHS · AI-09644 · United States
External Links
PubMed source DOI: 10.1073/pnas.87.2.743 PMC Full Text View journal details
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