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PMID: 3888290 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Overproduction of the membrane-bound components of the histidine permease from Salmonella typhimurium: identification of the M protein.

Biochimie ·Vol. 67 ·No. 1 ·1985-01-00 ·Pages 149-54

Ames GF, Nikaido K, Hobson A, Malcolm B

Abstract

The periplasmic histidine permease of Salmonella typhimurium is composed of a soluble histidine-binding protein and three membrane-bound components. These latter are produced in very small amounts and only two, the Q and the P protein, have been previously identified. This paper describes the construction of a plasmid carrying the hisQ, hisM, and hisP genes under the control of the lambda PL promoter, thus allowing great overproduction of those gene products. The M protein has been identified in such overproducing strains and its nature confirmed by constructing in vitro hisM deletions within the plasmid. With these results the identification of all components of the histidine permease has been completed.

MeSH Terms
ATP-Binding Cassette Transporters Amino Acid Transport Systems, Basic Bacterial Proteins Escherichia coli/genetics Genes, Bacterial Glycoproteins/biosynthesis,genetics Membrane Proteins/biosynthesis Membrane Transport Proteins/genetics,metabolism Operon Plasmids Salmonella typhimurium/enzymology
Chemicals
ATP-Binding Cassette Transporters Amino Acid Transport Systems, Basic Bacterial Proteins Glycoproteins Membrane Proteins Membrane Transport Proteins protein M (glycoprotein) histidine permease, Bacteria
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ames G F
Nikaido K
Hobson A
Malcolm B
Article Info
Journal
Biochimie
Abbr.
Biochimie
ISSN
0300-9084
Published
1985-01-00
Pages
149-54
Language
English
Region
France
NLM ID
1264604
Subset
IM
Grants
NIADDK NIH HHS · AM12121 · United States
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