Literature DB >> 6778869

Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system.

H A Shuman, T J Silhavy.   

Abstract

The malK gene product of Escherichia coli has been identified through the use of a previously described technique that employs gene fusions (Shuman, H. A., Silhavy, T. J., and Beckwith, J. R. (1980) J. Biol. Chem. 255, 168-174). This protein, along with the four other products of the malB locus, comprise the complete maltose transport system. The malK protein has a molecular weight of approximately 40,000 and is located in the cell envelope. In mutant strains which lack another component of the transport system, the malG protein, the malK protein is located in the cytoplasm. This alteration in location suggests that the malK protein is associated with the inner surface of the cytoplasmic membrane via an interaction with the malG protein.

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Year:  1981        PMID: 6778869

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  40 in total

1.  Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC transporter of the archaeon Thermococcus litoralis.

Authors:  K Diederichs; J Diez; G Greller; C Müller; J Breed; C Schnell; C Vonrhein; W Boos; W Welte
Journal:  EMBO J       Date:  2000-11-15       Impact factor: 11.598

2.  Cellular localization of the MalG protein from the maltose transport system in Escherichia coli K12.

Authors:  E Dassa
Journal:  Mol Gen Genet       Date:  1990-06

3.  The activities of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations.

Authors:  S Kühnau; M Reyes; A Sievertsen; H A Shuman; W Boos
Journal:  J Bacteriol       Date:  1991-04       Impact factor: 3.490

4.  The maltodextrin system of Escherichia coli: metabolism and transport.

Authors:  Renate Dippel; Winfried Boos
Journal:  J Bacteriol       Date:  2005-12       Impact factor: 3.490

Review 5.  Tinkering with transporters: periplasmic binding protein-dependent maltose transport in E. coli.

Authors:  H A Shuman; C H Panagiotidis
Journal:  J Bioenerg Biomembr       Date:  1993-12       Impact factor: 2.945

6.  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 7.  Uses of lac fusions for the study of biological problems.

Authors:  T J Silhavy; J R Beckwith
Journal:  Microbiol Rev       Date:  1985-12

8.  Study of regulation and transport of hemolysin by using fusion of the beta-galactosidase gene (lacZ) to hemolysin genes.

Authors:  A Juarez; M Härtlein; W Goebel
Journal:  J Bacteriol       Date:  1984-10       Impact factor: 3.490

9.  Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins.

Authors:  A L Davidson; H A Shuman; H Nikaido
Journal:  Proc Natl Acad Sci U S A       Date:  1992-03-15       Impact factor: 11.205

10.  Characterization of the mgl operon of Escherichia coli by transposon mutagenesis and molecular cloning.

Authors:  S Harayama; J Bollinger; T Iino; G L Hazelbauer
Journal:  J Bacteriol       Date:  1983-01       Impact factor: 3.490

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