A common assembly module in injectisome and flagellar type III secretion sorting platforms

被引:55
|
作者
Notti, Ryan Q. [1 ,2 ]
Bhattacharya, Shibani [3 ]
Lilic, Mirjana [1 ]
Stebbins, C. Erec [1 ]
机构
[1] Rockefeller Univ, Lab Struct Microbiol, New York, NY 10065 USA
[2] Weill Cornell Med Coll, Triinst Med Scientist Training Program, New York, NY 10021 USA
[3] New York Struct Biol Ctr, New York, NY 10027 USA
来源
NATURE COMMUNICATIONS | 2015年 / 6卷
基金
美国国家卫生研究院;
关键词
SALMONELLA-TYPHIMURIUM; BASAL BODY; RING COMPONENT; C-RING; PROTEIN; SYSTEMS; SOFTWARE; FEATURES; QUALITY; EXPORT;
D O I
10.1038/ncomms8125
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Translocating proteins across the double membrane of Gram-negative bacteria, type III secretion systems (T3SS) occur in two evolutionarily related forms: injectisomes, delivering virulence factors into host cells, and the flagellar system, secreting the polymeric filament used for motility. While both systems share related elements of a cytoplasmic sorting platform that facilitates the hierarchical secretion of protein substrates, its assembly and regulation remain unclear. Here we describe a module mediating the assembly of the sorting platform in both secretion systems, and elucidate the structural basis for segregation of homologous components among these divergent T3SS subtypes sharing a common cytoplasmic milieu. These results provide a foundation for the subtype-specific assembly of T3SS sorting platforms and will support further mechanistic analysis and anti-virulence drug design.
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收藏
页数:11
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