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PMID: 6407021 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Properties of the major outer membrane protein from Neisseria gonorrhoeae incorporated into model lipid membranes.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 80 ·No. 12 ·1983-06-00 ·Pages 3831-5

Young JD, Blake M, Mauro A, Cohn ZA

Abstract

The major outer membrane protein from Neisseria gonorrhoeae was incorporated into artificial planar bilayer membranes by a detergent-dilution procedure. The integrated protein forms voltage-dependent aqueous pores with a minimal pore diameter estimated to be 11 A. A pore of this size suggests a role for this protein in macromolecular sieving at the level of the outer membrane. This protein self-associates preferentially in triplets of three equal unit conductance steps of 130 pS (in 0.1 M NaCl) each. The two-state model may be applied to explain the voltage-dependent conductance. The average lifetime of the open state of single channels is strongly dependent on the applied voltage, the channels shifting to the closed state at higher voltages. The pore is anion selective, differing from porins of other Gram-negative bacteria studied so far but resembling the voltage-dependent anion-selective channel of the outer membrane of mitochondria.

MeSH Terms
Bacterial Proteins/metabolism Kinetics Lipid Bilayers Membrane Potentials Membrane Proteins/metabolism Neisseria gonorrhoeae/metabolism Permeability Phosphatidylcholines Phosphatidylethanolamines Proteolipids/metabolism
Chemicals
Bacterial Proteins Lipid Bilayers Membrane Proteins Phosphatidylcholines Phosphatidylethanolamines Proteolipids proteoliposomes
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Young J D
Blake M
Mauro A
Cohn Z A
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33 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.80.12.3831
Published
1983-06-00
Pages
3831-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC394146
Subset
IM
Grants
NCI NIH HHS · CA30198 · United States
External Links
PubMed source DOI: 10.1073/pnas.80.12.3831 PMC Full Text View journal details
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