JB Try JVI Online
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
JB.01084-06v1
188/24/8586    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 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 Kim, J.-S.
Right arrow Articles by Lee, J. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kim, J.-S.
Right arrow Articles by Lee, J. K.
Journal of Bacteriology, December 2006, p. 8586-8592, Vol. 188, No. 24
0021-9193/06/$08.00+0     doi:10.1128/JB.01084-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Lysine Decarboxylase Expression by Vibrio vulnificus Is Induced by SoxR in Response to Superoxide Stress{triangledown}

Ju-Sim Kim,1,{dagger} Sang Ho Choi,2 and Jeong K. Lee1*

Department of Life Science and Interdisciplinary Program of Integrated Biotechnology, Sogang University, Seoul 121-742, Korea,1 School of Agricultural Biotechnology and Center for Agricultural Biomaterials, Seoul National University, Seoul 151-742, Korea2

Received 22 July 2006/ Accepted 18 September 2006

Lysine decarboxylase expression by Vibrio vulnificus, which is up-regulated by CadC in response to acid stress, is also induced by SoxR in response to superoxide stress. SoxR binds to the promoter region of the cadBA operon, coding for a lysine-cadaverine antiporter (CadB) and a lysine decarboxylase (CadA). The induction of cadBA transcription by SoxR is independent of CadC. Cadaverine, which neutralizes the external medium, also appears to scavenge superoxide radicals, since increasing cellular cadaverine by elevating the gene dosage of cadBA significantly diminished the induction of Mn-containing superoxide dismutase under methyl viologen-induced oxidative stress. Consistently, a lack of cadaverine caused by mutation in cadA resulted in low tolerance to oxidative stress compared with that of the wild type.


* Corresponding author. Mailing address: Department of Life Science and Interdisciplinary Program of Integrated Biotechnology, Sogang University, Seoul 121-742, Korea. Phone: 82-2-705-8459. Fax: 82-2-704-3601. E-mail: jgklee{at}sogang.ac.kr.

{triangledown} Published ahead of print on 29 September 2006.

{dagger} Present address: Department of Microbiology, University of Colorado Health Science Center, Aurora, CO 80045.


Journal of Bacteriology, December 2006, p. 8586-8592, Vol. 188, No. 24
0021-9193/06/$08.00+0     doi:10.1128/JB.01084-06
Copyright © 2006, 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 © 2006 by the American Society for Microbiology. All rights reserved.