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Division of Tropical Animal production. Commonwealth Scientific and Industrial Research Organisation, Private Bag no. 3 PO, Indooroopilly, Qld 4068, Australia
Author for correspondence: Brian P. Dalrymple. Tel: +61 7 3214 2807. Fax: + 617 3214 2882. e-mail: b.dalrymple@:dance.tap.csiro.au
ABSTRACT
A second cinnamoyl ester hydrolase (CEH) encoding gene (cinB) has been characterized from the ruminal bacterium Butyrivibrio fibrisolvens E14. CinB is more similar to CinA (previously named Cinl) (28% amino acid identity), the first CEH described from B. fibrisolvens E14, than either of the enzymes are to any other member of the family of hydrolases to which they belong. Upstream of cinB, and in the opposite orientation, is a gene (cinR) encoding a protein with substantial similarity to members of the MarR family of negative regulators of bacterial gene expression. By alignment of these sequences, a possible helix-turn-helix DNA-binding domain has been identified. CinR was expressed at a high level in Escherichia coli using the lac promoter. In E. coli CinR repressed the expression of CinB, but had no effect on the expression of CinA. In gel mobility-shift assays, CinR bound specifically to the cinR-cinB intergenic region. Two identical 16 nucleotide inverted repeats adjacent to the putative PcinR and PcinB promoters are likely binding sites for CinR. The addition of FAXX (O-[5-O-(trans-feruloyl)-
-L-arabinofuranosyl]-(1,3)-O-ß-D-xylopyranosyl-(1,4)-D-xylopyranose) and Fara [5-O-(trans-feruloyl)-arabinofuranose], but not xylobiose, ferulic acid and a number of other soluble components of hemicellulose, inhibited the binding of CinR to DNA.
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