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PMID: 7035438 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Secretion and processing of ribose-binding protein in Escherichia coli.

Journal of bacteriology ·Vol. 149 ·No. 2 ·1982-02-00 ·Pages 789-92

Garwin JL, Beckwith J

Abstract

The periplasmic D-ribose-binding protein of Escherichia coli K-12 is made initially as a larger precursor form. This precursor was observed in wild-type cells and more stably in cells inhibited for protein secretion. The precursor could be processed to the mature D-ribose-binding protein either co-or posttranslationally. The secretion pathway of the D-ribose-binding protein and that of the maltose-binding secretion have many characteristics in common.

MeSH Terms
Bacterial Proteins/metabolism Carrier Proteins/metabolism Escherichia coli/genetics,metabolism Escherichia coli Proteins Molecular Weight Mutation Periplasmic Binding Proteins Protein Biosynthesis Protein Precursors/metabolism
Chemicals
Bacterial Proteins Carrier Proteins Escherichia coli Proteins Periplasmic Binding Proteins Protein Precursors RbsB protein, E coli
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Garwin J L
Beckwith J
References (9)
9 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1982-02-00
Pages
789-92
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC216576
Subset
IM
Grants
NIGMS NIH HHS · R01-GM13017 · United States
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