Literature DB >> 18643933

A new way out: protein localization on the bacterial cell surface via Tat and a novel Type II secretion system.

Sarah J Coulthurst1, Tracy Palmer.   

Abstract

SUMMARY: The ability to move proteins out of the cytoplasm and across membranes is a key aspect of the physiology and pathogenicity of Gram-negative bacteria. In this issue of Molecular Microbiology, Ferrandez and Condemine describe a novel protein targeting system in the enteric phytopathogen, Dickeya dadantii. The pectin lyase, PnlH, is exported by the Tat system and is somehow targeted to the outer membrane by its uncleaved N-terminal Tat signal anchor. A novel Type II secretion system, Stt, is then responsible for moving it across the outer membrane, where it remains localized on the surface of the cell. We discuss the implications of these findings for our understanding of both the mechanisms and physiological importance of bacterial protein targeting.

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Year:  2008        PMID: 18643933     DOI: 10.1111/j.1365-2958.2008.06367.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  5 in total

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4.  Isolation and Genome Analysis of Pectobacterium colocasium sp. nov. and Pectobacterium aroidearum, Two New Pathogens of Taro.

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5.  Assembly of the type II secretion system such as found in Vibrio cholerae depends on the novel Pilotin AspS.

Authors:  Rhys A Dunstan; Eva Heinz; Lakshmi C Wijeyewickrema; Robert N Pike; Anthony W Purcell; Timothy J Evans; Judyta Praszkier; Roy M Robins-Browne; Richard A Strugnell; Konstantin V Korotkov; Trevor Lithgow
Journal:  PLoS Pathog       Date:  2013-01-10       Impact factor: 6.823

  5 in total

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