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PMID: 273906 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Synthesis of phage M13 coat protein and its assembly into membranes in vitro.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 4 ·1978-04-00 ·Pages 1754-8

Wickner W, Mandel G, Zwizinski C, Bates M, Killick T

Abstract

The coat protein (gene 8 product) of coliphage M1O is an integral protein of the host cell membrane at all stages of virus infection. This protein, when made in a cell-free reaction, has been shown by others to have an additional NH2-terminal peptide region and is referred to as "procoat." It is initially not membrane-bound but, upon exposure to Escherichia coli membrane vesicles or to liposomes prepared from E. coli lipids, it assembles into the bilayer in an integral fashion. Much of this protein is shown to be exposed on the inner surface of the liposome. We suggest that refolding of procoat as it encounters the bilayer is sufficient to transport large segments of the peptide chain through the apolar hydrocarbon core.

MeSH Terms
Cell-Free System Coliphages/metabolism Kinetics Liposomes Membrane Proteins/metabolism Membranes/metabolism,ultrastructure Protein Precursors/metabolism Solubility Viral Proteins/biosynthesis,metabolism Virus Replication
Chemicals
Liposomes Membrane Proteins Protein Precursors Viral Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Wickner W
Mandel G
Zwizinski C
Bates M
Killick T
References (21)
21 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.75.4.1754
Published
1978-04-00
Pages
1754-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC392418
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.4.1754 PMC Full Text View journal details
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