Brinkworth, A.J. and Malcolm, D.S. and Pedrosa, A.T. and Roguska, K. and Shahbazian, S. and Graham, J.E. and Hayward, Richard D. and Carabeo, R.A. (2011) Chlamydia trachomatis Slc1 is a type III secretion chaperone that enhances the translocation of its invasion effector substrate TARP. Molecular Microbiology 82 (1), pp. 131-144. ISSN 0950-382X.
Abstract
Bacterial type III secretion system (T3SS) chaperones pilot substrates to the export apparatus in a secretion-competent state, and are consequently central to the translocation of effectors into target cells. Chlamydia trachomatis is a genetically intractable obligate intracellular pathogen that utilizes T3SS effectors to trigger its entry into mammalian cells. The only well-characterized T3SS effector is TARP (translocated actin recruitment protein), but its chaperone is unknown. Here we exploited a known structural signature to screen for putative type III secretion chaperones encoded within the C. trachomatis genome. Using bacterial two-hybrid, co-precipitation, cross-linking and size exclusion chromatography we show that Slc1 (SycE-like chaperone 1; CT043) specifically interacts with a 200-amino-acid residue N-terminal region of TARP (TARP1–200). Slc1 formed homodimers in vitro, as shown in cross-linking and gel filtration experiments. Biochemical analysis of an isolated Slc1–TARP1–200 complex was consistent with a characteristic 2:1 chaperone–effector stoichiometry. Furthermore, Slc1 was co-immunoprecipitated with TARP from C. trachomatis elementary bodies. Also, coexpression of Slc1 specifically enhanced host cell translocation of TARP by a heterologous Yersinia enterocolitica T3SS. Taken together, we propose Slc1 as a chaperone of the C. trachomatis T3SS effector TARP.
Metadata
Item Type: | Article |
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School: | Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences |
Research Centres and Institutes: | Structural Molecular Biology, Institute of (ISMB) |
Depositing User: | Administrator |
Date Deposited: | 16 May 2013 09:31 |
Last Modified: | 02 Aug 2023 17:04 |
URI: | https://eprints.bbk.ac.uk/id/eprint/6785 |
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