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PMID: 6997295 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Identification of a cytoplasmic membrane-associated component of the maltose transport system of Escherichia coli.

The Journal of biological chemistry ·Vol. 255 ·No. 18 ·1980-09-25 ·Pages 8366-9

Bavoil P, Hofnung M, Nikaido H

Abstract

The maltose transport system of Escherichia coli contains at least five components, three of which, i.e. the products of lamB, malE, and malF genes, have so far been identified as constituents of the outer membrane, periplasmic space, and cytoplasmic membrane, respectively. We identified another component, a cytoplasmic membrane protein of an apparent molecular weight of 43,000, as the product of the malK gene on the basis of polyacrylamide gel electrophoretic analysis of various mutants and suppressed strains and by the incorporation of extra tyrosine residue into this proten in malK amber mutants containing the suppressor Su3+ allele. The transport of maltose thus appears to require at least two proteins associated with the cytoplasmic membrane.

MeSH Terms
Alleles Biological Transport Cell Membrane/metabolism Escherichia coli/genetics,metabolism Genotype Maltose/metabolism Membrane Proteins/genetics,metabolism Mutation Suppression, Genetic
Chemicals
Membrane Proteins Maltose
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bavoil P
Hofnung M
Nikaido H
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1980-09-25
Pages
8366-9
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · 5-F32-GM07232 · United States
NIAID NIH HHS · AI 09644 · United States
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