Document Detail


M13 procoat inserts into liposomes in the absence of other membrane proteins.
MedLine Citation:
PMID:  3902814     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Procoat, the precursor form of the major coat protein of coliphage M13, assembles into the Escherichia coli inner membrane and is cleaved to mature coat protein by leader peptidase. This assembly process has previously been reconstituted using lipids and purified leader peptidase in a cell-free protein synthesis reaction (Watts, C., Silver, P., and Wickner, W. (1981) Cell 25, 347-353; Ohno-Iwashita, Y., and Wickner, W. (1983) J. Biol. Chem. 258, 1895-1900). We now report that procoat can also cross a liposomal membrane composed of only purified phospholipids; leader peptidase is not needed to catalyze insertion. When procoat is synthesized in vitro in the presence of liposomes with encapsulated chymotrypsin, the procoat inserts spontaneously through the membrane and is degraded. The protease was shown by several criteria to be in the lumen of the liposomes. These results demonstrate that the precursor form of an E. coli integral membrane protein can cross a membrane without the aid of leader peptidase or any other membrane proteins.
Authors:
B L Geller; W Wickner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  260     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1985 Oct 
Date Detail:
Created Date:  1985-11-29     Completed Date:  1985-11-29     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  13281-5     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Capsid / metabolism*
Capsid Proteins*
Chymotrypsin / metabolism
Coliphages
Endopeptidase K
Endopeptidases / metabolism,  physiology
Escherichia coli / metabolism
Liposomes / metabolism*
Membrane Proteins / physiology*
Oligopeptides / pharmacology
Phospholipids / metabolism
Protease Inhibitors / pharmacology
Protein Precursors / metabolism*
Serine Endopeptidases*
Chemical
Reg. No./Substance:
0/Capsid Proteins; 0/Liposomes; 0/Membrane Proteins; 0/Oligopeptides; 0/Phospholipids; 0/Protease Inhibitors; 0/Protein Precursors; 0/coat protein, Bacteriophage M13; 9076-44-2/chymostatin; EC 3.4.-/Endopeptidases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.1/Chymotrypsin; EC 3.4.21.64/Endopeptidase K; EC 3.4.21.89/type I signal peptidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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