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| Subject Categories: Microbiology & Pathogens |
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| The EMBO Journal
(2006) 25, 3223–3233, doi:10.1038/sj.emboj.7601202 Published online 22 June 2006 |
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| The discovery of SycO highlights a new function for type III secretion effector chaperones |
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| Michel Letzelter1, Isabel Sorg1, Luís Jaime Mota1, 3, Salome Meyer1, Jacqueline Stalder1, Mario Feldman1, 4, Marina Kuhn1, Isabelle Callebaut2 and Guy R Cornelis1 |
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1 Biozentrum der Universität Basel, Basel, Switzerland 2 Département de Biologie Structurale, Institut de Minéralogie et de Physique des Milieux Condensés (CNRS/UMR 7590) Universités Paris 6 & Paris 7, Paris, France To whom correspondence should be addressed Guy R Cornelis, Biozentrum, Klingelbergstrasse 50, 4056 Basel, Switzerland. Tel.: +41 61 267 2110; Fax: +41 61 267 2118; E-mail: guy.cornelis@unibas.ch 3 Present address: Imperial College London, Centre for Molecular Microbiology and Infection, Flowers Building, Armstrong Road, London SW7 2AZ, UK 4 Present address: Department of Biological Sciences, University of Alberta, Edmonton, Canada Received 11 January 2006; Accepted 29 May 2006; Published online 22 June 2006. |
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| Abstract |
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| Bacterial injectisomes deliver effector proteins straight into the cytosol of eukaryotic cells (type III secretion, T3S). Many effectors are associated with a specific chaperone that remains inside the bacterium when the effector is delivered. The structure of such chaperones and the way they interact with their substrate is well characterized but their main function remains elusive. Here, we describe and characterize SycO, a new chaperone for the Yersinia effector kinase YopO. The chaperone-binding domain (CBD) within YopO coincides with the membrane localization domain (MLD) targeting YopO to the host cell membrane. The CBD/MLD causes intrabacterial YopO insolubility and the binding of SycO prevents this insolubility but not folding and activity of the kinase. Similarly, SycE masks the MLD of YopE and SycT covers an aggregation-prone domain of YopT, presumably corresponding to its MLD. Thus, SycO, SycE and most likely SycT mask, inside the bacterium, a domain needed for proper localization of their cognate effector in the host cell. We propose that covering an MLD might be an essential function of T3S effector chaperones. |
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| Keywords: effectors, targeting, translocation, type III secretion, Yops |
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Top of page MORE ARTICLES LIKE THISThese links to content published by NPG are automatically generated NEWS AND VIEWSNature Medicine News and Views (01 Jan 2001) Nature Structural Biology News and Views (01 Dec 2001) RESEARCHTyeA, a protein involved in control of Yop release and in translocation of Yersinia Yop effectors The EMBO Journal Article (01 Apr 1998) |
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