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PMID: 54916 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S.

Asymmetric orientation of a phage coat protein in cytoplasmic membrane of Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 72 ·No. 12 ·1975-12-00 ·Pages 4749-53

Wickner W

Abstract

The coat protein of a filamentous phage (M13) enters the cytoplasmic membrane from two directions: from the outside upon infection and from the cell interior late in the viral life cycle prior to phage assembly and extrusion. Binding of 125I-labeled anti-coat protein antibody to spheroplasts or to inverted vesicles was used to assay the orientation of coat protein in the membrane. Both parental and newly synthesized coat protein were found to be exposed on the outer surface of the cytoplasmic membrane. Coat protein in intact infected cells is also accessible to external antibody. Thus two different processes of assembling a protein into membrane, each starting from a different membrane surface, appear to produce similar surface orientations.

MeSH Terms
Cell Membrane/metabolism,ultrastructure Coliphages/metabolism,ultrastructure Epitopes Escherichia coli/metabolism,ultrastructure Protein Conformation Spheroplasts/ultrastructure Viral Proteins/analysis,biosynthesis,immunology
Chemicals
Epitopes Viral Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Wickner W
References (32)
32 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.72.12.4749
Published
1975-12-00
Pages
4749-53
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC388808
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.72.12.4749 PMC Full Text View journal details
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