JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] --
JB Accepts, published online ahead of print on 11 May 2007
This Article
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
JB.00061-07v1
189/14/5153    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mashimo, T.
Right arrow Articles by Aizawa, S.-I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mashimo, T.
Right arrow Articles by Aizawa, S.-I.

 Previous Article  |  Next Article 

J. Bacteriol. doi:10.1128/JB.00061-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Temperature hyper-sensitive sites of the flagellar switch component FliG in Salmonella enterica serovar Typhimurium

Takuji Mashimo, Manami Hashimoto, Shigeru Yamaguchi, and Shin-Ichi Aizawa*

CREST, Japan Science & Technology Agency, c/o Innovation Plaza Hiroshima, 3-10-23 Kagamiyama, Higashi-Hiroshima, 739-0046 Japan; Prefectural University of Hiroshima, Department of Life Sciences, 562 Nanatsuka, Shobara, Hiroshima 727-0023, Japan

* To whom correspondence should be addressed. Email: aizawa{at}pu-hiroshima.ac.jp.


   Abstract

Three flagellar proteins, FliG, FliM, FliN (FliGMN), are the components of the C ring of the flagellar motor. The genes encoding these proteins are multifunctional; they show three different phenotypes (Fla-, Mot-, and Che-), depending on the site and type of the mutations. Some of the Mot- mutants previously characterized are found to be motile. Reexamination of all Mot- mutants in fliGMN genes so far studied revealed that many of them are actually temperature sensitive (TS); that is, they are motile at 20 C but non-motile at 37 C. There were two types of TS mutants: one caused a loss of function that was not reversed by a return to the permissive temperature (rigid TS) and the other caused a loss that was reversed (hyper-TS). The rigid TS mutants showed an all-or-none phenotype; that is, once a structure was formed, the structure and function were stable against temperature shifts. All of fliM and fliN and most of fliG TS mutants belong to this group. On the other hand, the hyper-TS mutants (three of the fliG mutants) showed a temporal swimming/stop phenotype, responding to temporal temperature shifts when the structure was formed at a permissive temperature. Those hyper-TS mutation sites are localized in the C-terminal domain of the FliG molecules at sites that are different from the previously proposed functional sites. We discuss a role of this new region of FliG in torque generation of the flagellar motor.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2007 by the American Society for Microbiology. All rights reserved.