| Literature DB >> 25488302 |
Chi-Lin Tsai1, Brianne J Burkinshaw2, Natalie C J Strynadka3, John A Tainer4.
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.Entities:
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Year: 2014 PMID: 25488302 PMCID: PMC4334186 DOI: 10.1128/JB.02524-14
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490