JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Yoshida, K.-i.
Right arrow Articles by Fujita, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yoshida, K.-i.
Right arrow Articles by Fujita, Y.

 Previous Article  |  Next Article 

Journal of Bacteriology, September 2004, p. 5640-5648, Vol. 186, No. 17
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.17.5640-5648.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Bacillus subtilis LmrA Is a Repressor of the lmrAB and yxaGH Operons: Identification of Its Binding Site and Functional Analysis of lmrB and yxaGH

Ken-ichi Yoshida,1* Yo-hei Ohki,1 Makiko Murata,2 Masaki Kinehara,1 Hiroshi Matsuoka,1 Takenori Satomura,1 Reiko Ohki,2 Miyuki Kumano,3 Kunio Yamane,3 and Yasutaro Fujita1

Department of Biotechnology, Fukuyama University, Fukuyama, Hiroshima,1 Department of Molecular Biology, School of Health Sciences, Kyorin University, Hachioji, Tokyo,2 Institute of Biological Science, University of Tsukuba, Tsukuba, Ibaragi, Japan3

Received 15 January 2004/ Accepted 2 June 2004

The Bacillus subtilis lmrAB operon is involved in multidrug resistance. LmrA is a repressor of its own operon, while LmrB acts as a multidrug efflux transporter. LmrA was produced in Escherichia coli cells and was shown to bind to the lmr promoter region, in which an LmrA-binding site was identified. Genome-wide screening involving DNA microarray analysis allowed us to conclude that LmrA also repressed yxaGH, which was not likely to contribute to the multidrug resistance. LmrA bound to a putative yxaGH promoter region, in which two tandem LmrA-binding sites were identified. The LmrA regulon was thus determined to comprise lmrAB and yxaGH. All three LmrA-binding sites contained an 18-bp consensus sequence, TAGACCRKTCWMTATAWT, which could play an important role in LmrA binding.


* Corresponding author. Present address: Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe 657-8501, Japan. Phone: 81 78-803-5862. Fax: 81 78-803-5815. E-mail: kenyoshi{at}kobe-u.ac.jp.


Journal of Bacteriology, September 2004, p. 5640-5648, Vol. 186, No. 17
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.17.5640-5648.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




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

Copyright © 2004 by the American Society for Microbiology. All rights reserved.