Interaction of the maltose-binding protein with membrane vesicles of Escherichia coli.

Journal of bacteriology ·Vol. 149 ·No. 2 ·1982-02-00 ·Pages 662-7

Richarme G

Abstract

The interaction of the radioactively labeled purified maltose-binding protein of Escherichia coli with membrane vesicles was studied. The maltose-binding protein bound specifically to the vesicles, in the presence of maltose, on few sites. Under conditions in which a potential was imposed across the membrane, the specific binding was (i) increased, (ii) dependent on maltose, and (iii) abolished in a mutant defective in the tar gene product, one of the methyl-accepting chemotaxis proteins. At least 1,300 binding sites were present in the membrane fraction of logarithmically growing cells.

MeSH Terms

ATP-Binding Cassette Transporters Bacterial Proteins/metabolism Binding Sites Carrier Proteins/metabolism Cell Membrane/metabolism Chemotaxis Escherichia coli/metabolism Escherichia coli Proteins Maltose/pharmacology Maltose-Binding Proteins Membrane Potentials Monosaccharide Transport Proteins Mutation Valinomycin/pharmacology

Chemicals

ATP-Binding Cassette Transporters Bacterial Proteins Carrier Proteins Escherichia coli Proteins Maltose-Binding Proteins Monosaccharide Transport Proteins maltose transport system, E coli Valinomycin Maltose

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Richarme G

References (33)

33 references, click to expand

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Article Info

Journal

Journal of bacteriology

Abbr.

J Bacteriol

ISSN

0021-9193

DOI

10.1128/jb.149.2.662-667.1982

Published

1982-02-00

Pages

662-7

Language

English

Region

United States

NLM ID

2985120R

PMCID

PMC216556

Subset

External Links

PubMed source DOI: 10.1128/jb.149.2.662-667.1982 PMC Full Text View journal details

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Interaction of the maltose-binding protein with membrane vesicles of Escherichia coli.

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