Literature DB >> 14659543

Functional complementation of E. coli secD and secG mutants by Helicobacter pylori homologues.

Nicola Fitchen1, Paul Williams, Kim R Hardie.   

Abstract

The Sec machinery is one mechanism used by bacteria to translocate proteins across their cytoplasmic membrane. Most of the Sec components have been identified within the important gastric pathogen, Helicobacter pylori, however their functionality has not yet been demonstrated. Here we report the existence of putative homologues to the Sec components yajC (HP1450) and yidC (HP1551), and demonstrate the ability of the H. pylori secD (HP1550) and secG (HP1255) homologues to facilitate inner membrane translocation of the maltose-binding protein MalE, by complementation of the respective secretion-deficient Escherichia coli mutants, thus providing evidence of their functionality.

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Year:  2003        PMID: 14659543     DOI: 10.1016/S0378-1097(03)00786-9

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  2 in total

Review 1.  Outer membrane biogenesis in Escherichia coli, Neisseria meningitidis, and Helicobacter pylori: paradigm deviations in H. pylori.

Authors:  George Liechti; Joanna B Goldberg
Journal:  Front Cell Infect Microbiol       Date:  2012-04-11       Impact factor: 5.293

2.  Understanding the dimorphic lifestyles of human gastric pathogen Helicobacter pylori using the SWATH-based proteomics approach.

Authors:  Mun Fai Loke; Chow Goon Ng; Yeespana Vilashni; Justin Lim; Bow Ho
Journal:  Sci Rep       Date:  2016-05-25       Impact factor: 4.379

  2 in total

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