Literature DB >> 12615213

The various and varying roles of specific chaperones in type III secretion systems.

Claude Parsot1, Cyril Hamiaux, Anne-Laure Page.   

Abstract

The type III secretion pathway is used by numerous Gram-negative pathogenic bacteria to deliver proteins within the membrane or the cytoplasm of eukaryotic cells with which these bacteria interact. Secretion is regulated by external signals. This requires that, before being secreted, proteins are stored in the cytoplasm where they need to be stabilised, separated from other interaction partners, and maintained in a secretion-competent state. Specialised, energy-independent chaperones play various roles in these functions by associating in the cytoplasm with proteins before their secretion. Some chaperones are also directly involved in modulating transcription in response to secretion.

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Year:  2003        PMID: 12615213     DOI: 10.1016/s1369-5274(02)00002-4

Source DB:  PubMed          Journal:  Curr Opin Microbiol        ISSN: 1369-5274            Impact factor:   7.934


  113 in total

Review 1.  Phages and the evolution of bacterial pathogens: from genomic rearrangements to lysogenic conversion.

Authors:  Harald Brüssow; Carlos Canchaya; Wolf-Dietrich Hardt
Journal:  Microbiol Mol Biol Rev       Date:  2004-09       Impact factor: 11.056

2.  Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity.

Authors:  André van Eerde; Cyril Hamiaux; Javier Pérez; Claude Parsot; Bauke W Dijkstra
Journal:  EMBO Rep       Date:  2004-04-16       Impact factor: 8.807

3.  Expression, purification, structural and functional analysis of SycB: a type three secretion chaperone from Yersinia enterocolitica.

Authors:  Abhishek Basu; Rakesh Chatterjee; Saumen Datta
Journal:  Protein J       Date:  2012-01       Impact factor: 2.371

4.  PEX5 protein binds monomeric catalase blocking its tetramerization and releases it upon binding the N-terminal domain of PEX14.

Authors:  Marta O Freitas; Tânia Francisco; Tony A Rodrigues; Inês S Alencastre; Manuel P Pinto; Cláudia P Grou; Andreia F Carvalho; Marc Fransen; Clara Sá-Miranda; Jorge E Azevedo
Journal:  J Biol Chem       Date:  2011-10-05       Impact factor: 5.157

Review 5.  Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.

Authors:  Daniela Büttner
Journal:  Microbiol Mol Biol Rev       Date:  2012-06       Impact factor: 11.056

6.  SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N-terminal secretion signal.

Authors:  Rasha Younis; Lewis E H Bingle; Sarah Rollauer; Diana Munera; Stephen J Busby; Steven Johnson; Janet E Deane; Susan M Lea; Gad Frankel; Mark J Pallen
Journal:  J Bacteriol       Date:  2010-09-10       Impact factor: 3.490

7.  Structural insight into the regulatory mechanisms of interactions of the flagellar type III chaperone FliT with its binding partners.

Authors:  Katsumi Imada; Tohru Minamino; Miki Kinoshita; Yukio Furukawa; Keiichi Namba
Journal:  Proc Natl Acad Sci U S A       Date:  2010-04-26       Impact factor: 11.205

Review 8.  Bacterial nanomachines: the flagellum and type III injectisome.

Authors:  Marc Erhardt; Keiichi Namba; Kelly T Hughes
Journal:  Cold Spring Harb Perspect Biol       Date:  2010-10-06       Impact factor: 10.005

9.  YspC: a unique translocator exhibits structural alteration in the complex form with chaperone SycB.

Authors:  Abhishek Basu; Rakesh Chatterjee; Saumen Datta
Journal:  Protein J       Date:  2012-08       Impact factor: 2.371

10.  Analysis of putative Chlamydia trachomatis chaperones Scc2 and Scc3 and their use in the identification of type III secretion substrates.

Authors:  Kenneth A Fields; Elizabeth R Fischer; David J Mead; Ted Hackstadt
Journal:  J Bacteriol       Date:  2005-09       Impact factor: 3.490

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