The flagellar-specific transcription factor, σ28, is the Type III secretion chaperone for the flagellar-specific anti-σ28 factor FlgM

被引:64
作者
Aldridge, Phillip D.
Karlinsey, Joyce E.
Aldridge, Christine
Birchall, Christopher
Thompson, Danielle
Yagasaki, Jin
Hughes, Kelly T.
机构
[1] Med Sch Newcastle Upon Tyne, Inst Cell & Mol Biosci, Newcastle Upon Tyne NE2 4HH, Tyne & Wear, England
[2] Univ Washington, Dept Microbiol, Seattle, WA 98195 USA
[3] Univ Utah, Dept Biol, Salt Lake City, UT 84112 USA
关键词
flagella; gene regulation; Type III secretion;
D O I
10.1101/gad.380406
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The sigma(28) protein is a member of the bacterial sigma(70)-family of transcription factors that directs RNA polymerase to flagellar late (class 3) promoters. The sigma(28) protein is regulated in response to flagellar assembly by the anti-sigma(28) factor FlgM. FlgM inhibits sigma(28)-dependent transcription of genes whose products are needed late in assembly until the flagellar basal motor structure, the hook-basal body (HBB), is constructed. A second function for the sigma(28) transcription factor has been discovered: sigma(28) facilitates the secretion of FlgM through the HBB, acting as the FlgM Type III secretion chaperone. Transcription-specific mutants in sigma(28) were isolated that remained competent for FlgM-facilitated secretion separating the transcription and secretion-facilitation activities of sigma(28). Conversely, we also describe the isolation of mutants in sigma(28) that are specific for FlgM-facilitated secretion. The data demonstrate that sigma(28) is the Type III secretion chaperone for its own anti-sigma factor FlgM. Thus, a novel role for a sigma(70)-family transcription factor is described.
引用
收藏
页码:2315 / 2326
页数:12
相关论文
共 48 条
[1]   Chaperone release and unfolding of substrates in type III secretion [J].
Akeda, Y ;
Galán, JE .
NATURE, 2005, 437 (7060) :911-915
[2]   Flk prevents premature secretion of the anti-σ factor FlgM into the periplasm [J].
Aldridge, P ;
Karlinsey, JE ;
Becker, E ;
Chevance, FFV ;
Hughes, KT .
MOLECULAR MICROBIOLOGY, 2006, 60 (03) :630-642
[3]   Cell cycle-dependent degradation of a flagellar motor component requires a novel-type response regulator [J].
Aldridge, P ;
Jenal, U .
MOLECULAR MICROBIOLOGY, 1999, 32 (02) :379-391
[4]   Type III secretion chaperone FlgN regulates flagellar assembly via a negative feedback loop containing its chaperone substrates FlgK and FlgL [J].
Aldridge, P ;
Karlinsey, J ;
Hughes, KT .
MOLECULAR MICROBIOLOGY, 2003, 49 (05) :1333-1345
[5]   Regulation of flagellar assembly [J].
Aldridge, P ;
Hughes, KT .
CURRENT OPINION IN MICROBIOLOGY, 2002, 5 (02) :160-165
[6]  
[Anonymous], 1980, ADV BACTERIAL GENET
[7]   Flagellin polymerisation control by a cytosolic export chaperone [J].
Auvray, F ;
Thomas, J ;
Fraser, GM ;
Hughes, C .
JOURNAL OF MOLECULAR BIOLOGY, 2001, 308 (02) :221-229
[8]   Prokaryotic motility structures [J].
Bardy, SL ;
Ng, SYM ;
Jarrell, KF .
MICROBIOLOGY-SGM, 2003, 149 :295-304
[9]   From flagellum assembly to virulence: the extended family of type III export chaperones [J].
Bennett, JCQ ;
Hughes, C .
TRENDS IN MICROBIOLOGY, 2000, 8 (05) :202-204
[10]  
BERG HC, 1973, NATURE, V245, P380, DOI 10.1038/245380a0