Previous Article | Next Article ![]()
Journal of Bacteriology, February 2005, p. 847-853, Vol. 187, No. 3
0021-9193/05/$08.00+0 doi:10.1128/JB.187.3.847-853.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
-Hexachlorocyclohexane in Sphingomonas paucimobilis UT26
Department of Environmental Life Sciences, Graduate School of Life Sciences, Tohoku University, Sendai,1 Department of Bioengineering, Nagaoka University of Technology, Kamitomioka, Nagaoka, Niigata, Japan2
Received 25 August 2004/ Accepted 2 November 2004
Sphingomonas paucimobilis UT26 utilizes
-hexachlorocyclohexane (
-HCH) as a sole source of carbon and energy. In our previous study, we cloned and characterized genes that are involved in the conversion of
-HCH to maleylacetate (MA) via chlorohydroquinone (CHQ) in UT26. In this study, we identified and characterized an MA reductase gene, designated linF, that is essential for the utilization of
-HCH in UT26. A gene named linEb, whose deduced product showed significant identity to LinE (53%), was located close to linF. LinE is a novel type of ring cleavage dioxygenase that catalyzes the conversion of CHQ to MA. LinEb expressed in Escherichia coli transformed CHQ and 2,6-dichlorohydroquinone to MA and 2-chloromaleylacetate, respectively. Our previous and present results indicate that UT26 (i) has two gene clusters for degradation of chlorinated aromatic compounds via hydroquinone-type intermediates and (ii) uses at least parts of both clusters for
-HCH utilization.
This article has been cited by other articles:
| Appl. Environ. Microbiol. | Infect. Immun. | Eukaryot. Cell |
|---|---|---|
| Mol. Cell. Biol. | J. Virol. | Microbiol. Mol. Biol. Rev. |
| ALL ASM JOURNALS |