Literature DB >> 2651120

Identification and localization of the membrane-associated, ATP-binding subunit of the oligopeptide permease of Salmonella typhimurium.

M P Gallagher1, S R Pearce, C F Higgins.   

Abstract

The OppF protein, a component of the oligopeptide permease of Salmonella typhimurium, is an ATP-binding protein and is believed to couple ATP hydrolysis to the transport process. This protein is an example of a large family of closely related proteins which couple ATP to a variety of different biological processes. The oppF gene has been cloned and sequenced. In order to identify and characterize its protein product we overproduced the protein from the cloned gene. Anti-OppF antibodies were raised against a synthetic peptide. Using these antibodies as a probe we identified OppF in wild-type and overproducing strains. Protease accessibility studies showed the protein to be a peripheral membrane protein located on the cytoplasmic side of the inner membrane. These findings have general implications for the organization and function of this class of prokaryotic and eukaryotic transport system.

Entities:  

Mesh:

Substances:

Year:  1989        PMID: 2651120     DOI: 10.1111/j.1432-1033.1989.tb14623.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  17 in total

1.  Subcellular localization of the Rhizobium leguminosarum nodI gene product.

Authors:  H R Schlaman; R J Okker; B J Lugtenberg
Journal:  J Bacteriol       Date:  1990-09       Impact factor: 3.490

2.  Energy coupling to periplasmic binding protein-dependent transport systems: stoichiometry of ATP hydrolysis during transport in vivo.

Authors:  M L Mimmack; M P Gallagher; S R Pearce; S C Hyde; I R Booth; C F Higgins
Journal:  Proc Natl Acad Sci U S A       Date:  1989-11       Impact factor: 11.205

3.  Polymorphism in a second ABC transporter gene located within the class II region of the human major histocompatibility complex.

Authors:  S H Powis; I Mockridge; A Kelly; L A Kerr; R Glynne; U Gileadi; S Beck; J Trowsdale
Journal:  Proc Natl Acad Sci U S A       Date:  1992-02-15       Impact factor: 11.205

4.  The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface.

Authors:  V Baichwal; D Liu; G F Ames
Journal:  Proc Natl Acad Sci U S A       Date:  1993-01-15       Impact factor: 11.205

Review 5.  Linkage map of Escherichia coli K-12, edition 10: the traditional map.

Authors:  M K Berlyn
Journal:  Microbiol Mol Biol Rev       Date:  1998-09       Impact factor: 11.056

Review 6.  Energy coupling in bacterial periplasmic permeases.

Authors:  G F Ames; A K Joshi
Journal:  J Bacteriol       Date:  1990-08       Impact factor: 3.490

7.  Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport.

Authors:  L Bishop; R Agbayani; S V Ambudkar; P C Maloney; G F Ames
Journal:  Proc Natl Acad Sci U S A       Date:  1989-09       Impact factor: 11.205

Review 8.  Binding protein-dependent transport systems.

Authors:  C F Higgins; S C Hyde; M M Mimmack; U Gileadi; D R Gill; M P Gallagher
Journal:  J Bioenerg Biomembr       Date:  1990-08       Impact factor: 2.945

9.  Functional exchangeability of the ABC proteins of the periplasmic binding protein-dependent transport systems Ugp and Mal of Escherichia coli.

Authors:  D Hekstra; J Tommassen
Journal:  J Bacteriol       Date:  1993-10       Impact factor: 3.490

10.  Iron(III)hydroxamate transport of Escherichia coli K12: single amino acid replacements at potential ATP-binding sites inactivate the FhuC protein.

Authors:  K Becker; W Köster; V Braun
Journal:  Mol Gen Genet       Date:  1990-08
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.