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Journal of Bacteriology, November 1999, p. 6712-6719, Vol. 181, No. 21
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Cloning and Sequencing of a Novel meta-Cleavage Dioxygenase Gene Whose Product Is Involved in Degradation of gamma -Hexachlorocyclohexane in Sphingomonas paucimobilis

Keisuke Miyauchi, Yugo Adachi, Yuji Nagata,* and Masamichi Takagi

Department of Biotechnology, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan

Received 19 April 1999/Accepted 18 August 1999

Sphingomonas (formerly Pseudomonas) paucimobilis UT26 utilizes gamma -hexachlorocyclohexane (gamma -HCH), a halogenated organic insecticide, as a sole source of carbon and energy. In a previous study, we showed that gamma -HCH is degraded to chlorohydroquinone (CHQ) and then to hydroquinone (HQ), although the rate of reaction from CHQ to HQ was slow (K. Miyauchi, S. K. Suh, Y. Nagata, and M. Takagi, J. Bacteriol. 180:1354-1359, 1998). In this study, we cloned and characterized a gene, designated linE, which is located upstream of linD and is directly involved in the degradation of CHQ. The LinE protein consists of 321 amino acids, and all of the amino acids which are reported to be essential for the activity of meta-cleavage dioxygenases are conserved in LinE. Escherichia coli overproducing LinE could convert both CHQ and HQ, producing gamma -hydroxymuconic semialdehyde and maleylacetate, respectively, with consumption of O2 but could not convert catechol, which is one of the major substrates for meta-cleavage dioxygenases. LinE seems to be resistant to the acylchloride, which is the ring cleavage product of CHQ and which seems to react with water to be converted to maleylacetate. These results indicated that LinE is a novel type of meta-cleavage dioxygenase, designated (chloro)hydroquinone 1,2-dioxygenase, which cleaves aromatic rings with two hydroxyl groups at para positions preferably. This study represents a direct demonstration of a new type of ring cleavage pathway for aromatic compounds, the hydroquinone pathway.

* Corresponding author. Mailing address: Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan. Phone: 81-3-5841-5178. Fax: 81-3-5841-8015. E-mail: aynaga{at}hongo.ecc.u-tokyo.ac.jp.

Journal of Bacteriology, November 1999, p. 6712-6719, Vol. 181, No. 21
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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