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J Bacteriol, May 1998, p. 2312-2320, Vol. 180, No. 9
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Cloning, Sequence Analysis, and Characterization of the Genes Involved in Isoprimeverose Metabolism in Lactobacillus pentosus

Stéphane Chaillou,1,2 B. Christien Lokman,2 Rob J. Leer,2 Clara Posthuma,1,2 Pieter W. Postma,1 and Peter H. Pouwels1,2,*

EC Slater Institute, Biocentrum, University of Amsterdam, 1018 TV Amsterdam,1 and TNO Nutrition and Food Research Institute, Department of Molecular Genetics and Gene technology, 3700 AJ Zeist,2 The Netherlands

Received 17 November 1997/Accepted 20 February 1998

Two genes, xylP and xylQ, from the xylose regulon of Lactobacillus pentosus were cloned and sequenced. Together with the repressor gene of the regulon, xylR, the xylPQ genes form an operon which is inducible by xylose and which is transcribed from a promoter located 145 bp upstream of xylP. A putative xylR binding site (xylO) and a cre-like element, mediating CcpA-dependent catabolite repression, were found in the promoter region. L. pentosus mutants in which both xylP and xylQ (LPE1) or only xylQ (LPE2) was inactivated retained the ability to ferment xylose but were impaired in their ability to ferment isoprimeverose (alpha -D-xylopyranosyl-(1,6)-D-glucopyranose). Disruption of xylQ resulted specifically in the loss of a membrane-associated alpha -xylosidase activity when LPE1 or LPE2 cells were grown on xylose. In the membrane fraction of wild-type bacteria, alpha -xylosidase could catalyze the hydrolysis of isoprimeverose and p-nitrophenyl-alpha -D-xylopyranoside with apparent Km and Vmax values of 0.2 mM and 446 nmol/min/mg of protein, and 1.3 mM and 54 nmol/min/mg of protein, respectively. The enzyme could also hydrolyze the alpha -xylosidic linkage in xyloglucan oligosaccharides, but neither methyl-alpha -D-xylopyranoside nor alpha -glucosides were substrates. Glucose repressed the synthesis of alpha -xylosidase fivefold, and 80% of this repression was released in an L. pentosus Delta ccpA mutant. The alpha -xylosidase gene was also expressed in the absence of xylose when xylR was disrupted.

* Corresponding author. Mailing address: TNO Nutrition and Food Research Institute, Department of Molecular Genetics and Gene- technology, P.O. Box 360, 3700 AJ Zeist, The Netherlands. Phone: 31 30 6944 462. Fax: 31 30 6944 466. E-mail: Pouwels{at}voeding.tno.nl.

J Bacteriol, May 1998, p. 2312-2320, Vol. 180, No. 9
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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