Flipping the switch: bringing order to flagellar assembly

被引:74
作者
Ferris, Hedda U.
Minamino, Tohru
机构
[1] Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06520 USA
[2] Osaka Univ, Grad Sch Frontier Biosci, Suita, Osaka 5650871, Japan
[3] JST, ICORP, Dynam Nanomachine Project, Suita, Osaka 5650871, Japan
关键词
D O I
10.1016/j.tim.2006.10.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The bacterial flagellum is a complex self-assembling nanomachine that contains its own type III protein export apparatus. Upon completion of early flagellar structure, this apparatus switches substrate specificity to export late structural subunits, thereby coupling sequential flagellar gene expression with flagellar assembly. The switch is achieved by a conformationall change of the export apparatus component FIhB driven by the flagellar hook-length control protein FliK. Two basic models of FliK- and FlhB-based switching are currently being pursued, together with the investigation of another factor, Flk, which prevents premature export of late substrates. Here, we review in detail each of these three export switch components and present the current understanding of how they work in concert in the making of a flagellum.
引用
收藏
页码:519 / 526
页数:8
相关论文
共 57 条
[1]  
ANDRIDGE P, 2006, MOL MICROBIOL, V60, P630
[2]  
BERG HC, 1973, NATURE, V245, P380, DOI 10.1038/245380a0
[3]   The flagellar hook protein, FlgE, of Salmonella enterica serovar typhimurium is posttranscriptionally regulated in response to the stage of flagellar assembly [J].
Bonifield, HR ;
Yamaguchi, S ;
Hughes, KT .
JOURNAL OF BACTERIOLOGY, 2000, 182 (14) :4044-4050
[4]   YscP and YscU regulate substrate specificity of the Yersinia type III secretion system [J].
Edqvist, PJ ;
Olsson, J ;
Lavander, M ;
Sundberg, L ;
Forsberg, Å ;
Wolf-Watz, H ;
Lloyd, SA .
JOURNAL OF BACTERIOLOGY, 2003, 185 (07) :2259-2266
[5]   BACTERIAL FLAGELLA - POLARITY OF ELONGATION [J].
EMERSON, SU ;
TOKYUASU, K ;
SIMON, MI .
SCIENCE, 1970, 169 (3941) :190-&
[6]   Enzymatic characterization of FliI - An ATPase involved in flagellar assembly in Salmonella typhimurium [J].
Fan, F ;
Macnab, RM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (50) :31981-31988
[7]   FlhB regulates ordered export of flagellar components via autocleavage mechanism [J].
Ferris, HU ;
Furukawa, Y ;
Minamino, T ;
Kroetz, MB ;
Kihara, M ;
Namba, K ;
Macnab, RM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (50) :41236-41242
[8]   Substrate specificity of type III flagellar protein export in Salmonella is controlled by subdomain interactions in FlhB [J].
Fraser, GM ;
Hirano, T ;
Ferris, HU ;
Devgan, LL ;
Kihara, M ;
Macnab, RM .
MOLECULAR MICROBIOLOGY, 2003, 48 (04) :1043-1057
[9]   Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway [J].
González-Pedrajo, B ;
Fraser, GM ;
Minamino, T ;
Macnab, RM .
MOLECULAR MICROBIOLOGY, 2002, 45 (04) :967-982
[10]   Substrate specificity classes and the recognition signal for Salmonella type III flagellar export [J].
Hirano, T ;
Minamino, T ;
Namba, K ;
Macnab, RM .
JOURNAL OF BACTERIOLOGY, 2003, 185 (08) :2485-2492