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Journal of Bacteriology, April 2003, p. 2219-2226, Vol. 185, No. 7
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.7.2219-2226.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Involvement of the Multidomain Regulatory Protein XynR in Positive Control of Xylanase Gene Expression in the Ruminal Anaerobe Prevotella bryantii B14

Kohji Miyazaki,1 Hiroyuki Miyamoto,1 Derry K. Mercer,2* Tatsuaki Hirase,1 Jennifer C. Martin,2 Yoichi Kojima,1 and Harry J. Flint2

Laboratory of Animal Science, Kyoto Prefectural University, Shimogamo, Kyoto 606-8522, Japan,1 Rowett Research Institute, Bucksburn, Aberdeen, AB21 9SB, United Kingdom2

Received 22 August 2002/ Accepted 2 January 2003

The xylanase gene cluster from the rumen anaerobe Prevotella bryantii B14 was found to include a gene (xynR) that encodes a multidomain regulatory protein and is downstream from the xylanase and ß-xylosidase genes xynA and xynB. Additional genes identified upstream of xynA and xynB include xynD, which encodes an integral membrane protein that has homology with Na:solute symporters; xynE, which is related to the genes encoding acylhydrolases and arylesterases; and xynF, which has homology with the genes encoding {alpha}-glucuronidases. XynR includes, in a single 833-amino-acid polypeptide, a putative input domain unrelated to other database sequences, a likely transmembrane domain, histidine kinase motifs, response regulator sequences, and a C-terminal AraC-type helix-turn-helix DNA binding domain. Two transcripts (3.7 and 5.8 kb) were detected with a xynA probe, and the start site of the 3.7-kb transcript encoding xynABD was mapped to a position upstream of xynD. The DNA binding domain of XynR was purified after amplification and overexpression in Escherichia coli and was found to bind to a 141-bp DNA fragment from the region immediately upstream of xynD. In vitro transcription assays demonstrated that XynR stimulates transcription of the 3.7-kb transcript. We concluded that XynR acts as a positive regulator that activates expression of xynABD in P. bryantii B14. This is the first regulatory protein that demonstrates significant homology with the two-component regulatory protein superfamily and has been shown to be involved in the regulation of polysaccharidase gene expression.

* Corresponding author. Mailing address: Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen, AB21 9SB, United Kingdom. Phone: 44 (0) 1224 716624. Fax: 44 (0) 1224 716687. E-mail: D.Mercer{at}rowett.ac.uk.

Journal of Bacteriology, April 2003, p. 2219-2226, Vol. 185, No. 7
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.7.2219-2226.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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