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PMID: 322142 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Amino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane.

Inouye S, Wang S, Sekizawa J, Halegoua S, Inouye M

Abstract

The messenger RNA for the lipoprotein of the E. coli outer membrane was found to code for a putative precursor, prolipoprotein, which has 20 additional amino acid residues extending from the amino terminus of the lipoprotein. Using the prolipoprotein synthesized in an E. coli cell-free system directed by purified messenger RNA for the lipoprotein, the complete amino acid sequence of the amino-terminal precursor region was determined to be as follows: (formula: see text). It was also found that the prolipoprotein that accumulates in toluene-treated cells has the same sequence. The significance of the amino acid sequence is discussed in terms of the mechanism of biosynthesis and assembly of the lipoprotein in the E. coli outer membrane.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/biosynthesis Cell Membrane/metabolism,ultrastructure Cell-Free System Escherichia coli/drug effects,ultrastructure Lipoproteins/biosynthesis Membrane Proteins/biosynthesis Molecular Weight Protein Precursors/biosynthesis Toluene/pharmacology
Chemicals
Bacterial Proteins Lipoproteins Membrane Proteins Protein Precursors Toluene
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Inouye S
Wang S
Sekizawa J
Halegoua S
Inouye M
References (17)
17 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
Published
1977-03-00
Pages
1004-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC430563
Subset
IM
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