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Applied and Environmental Microbiology, May 2000, p. 2125-2132, Vol. 66, No. 5
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Coexistence of Two Different O Demethylation Systems in Lignin Metabolism by Sphingomonas paucimobilis SYK-6: Cloning and Sequencing of the Lignin Biphenyl-Specific O-Demethylase (LigX) Gene

Tomonori Sonoki,1,* Takahiro Obi,1 Sachiko Kubota,1 Motoo Higashi,1 Eiji Masai,2 and Yoshihiro Katayama1

Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588,1 and Department of Bioengineering, Nagaoka University of Engineering, Kamitomioka, Nagaoka, Nigata 940-2188,2 Japan

Received 29 October 1999/Accepted 9 February 2000

Sphingomonas paucimobilis SYK-6 can grow on several dimeric model compounds of lignin as a carbon and energy source. It has O demethylation systems on three kinds of substrates: 5,5'-dehydrodivanillic acid (DDVA), syringate, and vanillate. We previously reported the cloning of a gene involved in the tetrahydrofolate-dependent O demethylation of syringate and vanillate. In the study reported here, we cloned the gene responsible for DDVA O demethylation. Using nitrosoguanidine mutagenesis, a mutant strain, NT-1, which could not degrade DDVA but could degrade syringate and vanillate, was isolated and was used to clone the gene responsible for the O demethylation of DDVA by complementation. Sequencing analysis showed an open reading frame (designated ligX) of 1,266 bp in this fragment. The deduced amino acid sequence of LigX had similarity to class I type oxygenases. LigX was involved in O demethylation activity on DDVA but not on vanillate and syringate. DDVA O demethylation activity in S. paucimobilis SYK-6 cell extracts was inhibited by addition of the LigX polyclonal antiserum. Thus, LigX is an essential enzyme for DDVA O demethylation in SYK-6. S. paucimobilis SYK-6 has two O demethylation systems: one is an oxygenative demethylase system, and the other is a tetrahydrofolate-dependent methyltransferase system.

* Corresponding author. Mailing address: Graduate School of Bio-Applications & Systems Engineering, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan. Phone and fax: 81-42-388-7364. E-mail: tomosono{at}cc.tuat.ac.jp.

Applied and Environmental Microbiology, May 2000, p. 2125-2132, Vol. 66, No. 5
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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