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J. Biol. Chem., Vol. 279, Issue 9, 8116-8125, February 27, 2004

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A Hexose Transporter Homologue Controls Glucose Repression in the Methylotrophic Yeast Hansenula polymorpha^*

Oleh V. Stasyk, Olena G. Stasyk, Janet Komduur¶, Marten Veenhuis¶, James M. Cregg||, and Andrei A. Sibirny**

From the Institute of Cell Biology, National Academy of Sciences of Ukraine, Drahomanov Street 14/16, Lviv 79005, Ukraine, the ^¶University of Groningen, Biological Centre, P. O. Box 14, 9750 AA Haren, The Netherlands, the ^||Keck Graduate Institute of Applied Life Sciences, 535 Watson Dr., Claremont, California 91711, and the ^**Rzeszów University, Cegelniana Street 12, 35-310 Rzeszów, Poland

Peroxisome biogenesis and synthesis of peroxisomal enzymes in the methylotrophic yeast Hansenula polymorpha are under the strict control of glucose repression. We identified an H. polymorpha glucose catabolite repression gene (HpGCR1) that encodes a hexose transporter homologue. Deficiency in GCR1 leads to a pleiotropic phenotype that includes the constitutive presence of peroxisomes and peroxisomal enzymes in glucose-grown cells. Glucose transport and repression defects in a UV-induced gcr1-2 mutant were found to result from a missense point mutation that substitutes a serine residue (Ser⁸⁵) with a phenylalanine in the second predicted transmembrane segment of the Gcr1 protein. In addition to glucose, mannose and trehalose fail to repress the peroxisomal enzyme, alcohol oxidase in gcr1-2 cells. A mutant deleted for the GCR1 gene was additionally deficient in fructose repression. Ethanol, sucrose, and maltose continue to repress peroxisomes and peroxisomal enzymes normally and therefore, appear to have GCR1-independent repression mechanisms in H. polymorpha. Among proteins of the hexose transporter family of baker's yeast, Saccharomyces cerevisiae, the amino acid sequence of the H. polymorpha Gcr1 protein shares the highest similarity with a core region of Snf3p, a putative high affinity glucose sensor. Certain features of the phenotype exhibited by gcr1 mutants suggest a regulatory role for Gcr1p in a repression pathway, along with involvement in hexose transport.

Received for publication, October 6, 2003 , and in revised form, December 1, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY465112.

^* This research was supported by International Association of European Union Grant 01-0583. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported in part by FIRCA Grant TW00547 from the National Institutes of Health, Fogarty International Center.

To whom correspondence should be addressed: Institute of Cell Biology, Drahomanov St. 14/16, Lviv 79005, Ukraine. Tel.: 380-322-740363; Fax: 380-322-721648; E-mail: sibirny{at}biochem.lviv.ua.

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