Literature DB >> 17126597

On the role of specific chaperones, the specific ATPase, and the proton motive force in type III secretion.

Gottfried Wilharm1, Svea Dittmann, Annika Schmid, Jürgen Heesemann.   

Abstract

Type III secretion systems (T3SSs) are engaged by a broad number of Gram-negative bacteria to inject proteins into host cells. The simultaneous crossing of three biological membranes by these proteins is a phenomenon which is far from being understood mechanistically. However, recent work from several groups has substantially enriched our conception of how proteins travel from the bacterial into the host cell cytosol. Here, we focus on the role of specific T3SS chaperones, the specific ATPase, and the proton motive force in type III secretion.

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Year:  2006        PMID: 17126597     DOI: 10.1016/j.ijmm.2006.10.003

Source DB:  PubMed          Journal:  Int J Med Microbiol        ISSN: 1438-4221            Impact factor:   3.473


  22 in total

Review 1.  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

2.  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

3.  Structural characterization of the Yersinia pestis type III secretion system needle protein YscF in complex with its heterodimeric chaperone YscE/YscG.

Authors:  Ping Sun; Joseph E Tropea; Brian P Austin; Scott Cherry; David S Waugh
Journal:  J Mol Biol       Date:  2008-01-05       Impact factor: 5.469

4.  Cross-talk between type three secretion system and metabolism in Yersinia.

Authors:  Annika Schmid; Wibke Neumayer; Konrad Trülzsch; Lars Israel; Axel Imhof; Manfred Roessle; Guido Sauer; Susanna Richter; Susan Lauw; Eva Eylert; Wolfgang Eisenreich; Jürgen Heesemann; Gottfried Wilharm
Journal:  J Biol Chem       Date:  2009-02-25       Impact factor: 5.157

5.  High-yield production of secreted active proteins by the Pseudomonas aeruginosa type III secretion system.

Authors:  M Derouazi; B Toussaint; L Quénée; O Epaulard; M Guillaume; R Marlu; B Polack
Journal:  Appl Environ Microbiol       Date:  2008-04-04       Impact factor: 4.792

6.  Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec System.

Authors:  Yihfen T Yen; Ravin Seepersaud; Barbara A Bensing; Paul M Sullam
Journal:  J Bacteriol       Date:  2011-04-29       Impact factor: 3.490

7.  Chaperone-mediated secretion switching from early to middle substrates in the type III secretion system encoded by Salmonella pathogenicity island 2.

Authors:  Akiko Takaya; Hikari Takeda; Shogo Tashiro; Hiroto Kawashima; Tomoko Yamamoto
Journal:  J Biol Chem       Date:  2019-01-16       Impact factor: 5.157

8.  Specific chaperones for the type VII protein secretion pathway.

Authors:  Maria H Daleke; Aniek D van der Woude; Annabel H A Parret; Roy Ummels; A Marit de Groot; David Watson; Sander R Piersma; Connie R Jiménez; Joen Luirink; Wilbert Bitter; Edith N G Houben
Journal:  J Biol Chem       Date:  2012-07-29       Impact factor: 5.157

Review 9.  Molecular pathogenesis of Shigella spp.: controlling host cell signaling, invasion, and death by type III secretion.

Authors:  Gunnar N Schroeder; Hubert Hilbi
Journal:  Clin Microbiol Rev       Date:  2008-01       Impact factor: 26.132

Review 10.  Timing is everything: the regulation of type III secretion.

Authors:  Janet E Deane; Patrizia Abrusci; Steven Johnson; Susan M Lea
Journal:  Cell Mol Life Sci       Date:  2009-12-31       Impact factor: 9.261

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