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J Bacteriol, March 1998, p. 1354-1359, Vol. 180, No. 6
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Cloning and Sequencing of a 2,5-Dichlorohydroquinone Reductive Dehalogenase Gene Whose Product Is Involved in Degradation of gamma -Hexachlorocyclohexane by Sphingomonas paucimobilis

Keisuke Miyauchi,1,* Seug-Kyo Suh,2 Yuji Nagata,1 and Masamichi Takagi1

Department of Biotechnology, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan,1 and Department of Environmental Management, Shinil Christian College, Susung-ku, Taegu 706-020, Korea2

Received 7 August 1997/Accepted 7 January 1998

Sphingomonas (formerly Pseudomonas) paucimobilis UT26 utilizes gamma -hexachlorocyclohexane (gamma -HCH), a halogenated organic insecticide, as a sole carbon and energy source. In a previous study, we showed that gamma -HCH is degraded to 2,5-dichlorohydroquinone (2,5-DCHQ) (Y. Nagata, R. Ohtomo, K. Miyauchi, M. Fukuda, K. Yano, and M. Takagi, J. Bacteriol. 176:3117-3125, 1994). In the present study, we cloned and characterized a gene, designated linD, directly involved in the degradation of 2,5-DCHQ. The linD gene encodes a peptide of 343 amino acids and has a low level of similarity to proteins which belong to the glutathione S-transferase family. When LinD was overproduced in Escherichia coli, a 40-kDa protein was found after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Northern blot analysis revealed that expression of the linD gene was induced by 2,5-DCHQ in S. paucimobilis UT26. Thin-layer chromatography and gas chromatography-mass spectrometry analyses with the LinD-overexpressing E. coli cells revealed that LinD converts 2,5-DCHQ rapidly to chlorohydroquinone (CHQ) and also converts CHQ slowly to hydroquinone. LinD activity in crude cell extracts was increased 3.7-fold by the addition of glutathione. All three of the Tn5-induced mutants of UT26, which lack 2,5-DCHQ dehalogenase activity, had rearrangements or a deletion in the linD region. These results indicate that LinD is a glutathione-dependent reductive dehalogenase involved in the degradation of gamma -HCH by S. paucimobilis UT26.

* Corresponding author. Mailing address: Department of Biotechnology, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan. Phone: 81-3-3812-2111, ext. 5178. Fax: 81-3-3812-9246. E-mail: aa67118{at}hongo.ecc.u-tokyo.ac.jp.




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