Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California, USA.
Department of Biochemistry and Molecular Biology and Center for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada.
J Bacteriol. 2015 Feb 15;197(4):672-5. doi: 10.1128/JB.02524-14. Epub 2014 Dec 8.
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.
细菌通过 III 型分泌系统 (T3SS) 将毒力效应蛋白注入宿主细胞质,从而劫持真核细胞。效应蛋白与其伴侣伴侣蛋白一起靶向六聚体 T3SS ATP 酶位于细菌膜胞质面。在本期《细菌学杂志》中,Roblin 等人(P. Roblin、F. Dewitte、V. Villeret、E. G. Biondi 和 C. Bompard,J Bacteriol 197:688-698, 2015, http://dx.doi.org/10.1128/JB.02294-14)表明,沙门氏菌的 T3SS 伴侣蛋白 SigE 与同源效应蛋白 SopB 结合时可以形成六聚体环,而不是二聚体,这意味着伴侣蛋白/效应蛋白复合物与其 ATP 酶形成了一种新的多聚体关联。