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J Bacteriol. 2015 Feb 15;197(4):672-5. doi: 10.1128/JB.02524-14. Epub 2014 Dec 8.

The Salmonella type III secretion system virulence effector forms a new hexameric chaperone assembly for export of effector/chaperone complexes.

Author information

1
Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA.
2
Department of Biochemistry and Molecular Biology and Center for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
3
Department of Biochemistry and Molecular Biology and Center for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada ncjs@mail.ubc.ca JATainer@lbl.gov.
4
Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA ncjs@mail.ubc.ca JATainer@lbl.gov.

Abstract

Bacteria hijack eukaryotic cells by injecting virulence effectors into host cytosol with a type III secretion system (T3SS). Effectors are targeted with their cognate chaperones to hexameric T3SS ATPase at the bacterial membrane's cytosolic face. In this issue of the Journal of Bacteriology, Roblin et al. (P. Roblin, F. Dewitte, V. Villeret, E. G. Biondi, and C. Bompard, J Bacteriol 197:688-698, 2015, http://dx.doi.org/10.1128/JB.02294-14) show that the T3SS chaperone SigE of Salmonella can form hexameric rings rather than dimers when bound to its cognate effector, SopB, implying a novel multimeric association for chaperone/effector complexes with their ATPase.

PMID:
25488302
PMCID:
PMC4334186
DOI:
10.1128/JB.02524-14
[Indexed for MEDLINE]
Free PMC Article

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