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J. Biol. Chem., Vol. 280, Issue 4, 2759-2770, January 28, 2005

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Transcriptional Regulation by Lge1p Requires a Function Independent of Its Role in Histone H2B Ubiquitination^*

Xiaoting Zhang¶, Ania Kolaczkowska||**, Frédéric Devaux, Sneh Lata Panwar||, Timothy C. Hallstrom||, Claude Jacq, and W. Scott Moye-Rowley||¶¶

From the ^||Department of Physiology and Biophysics and the Molecular Biology Graduate Program, University of Iowa, Iowa City, Iowa 52242 and the Laboratoire de Génétique Moléculaire, CNRS, Ecole Normale Supérieure, 75230 Paris, Cedex 05, France

Saccharomyces cerevisiae cells that have lost their mitochondrial genome (⁰) strongly induce transcription of multidrug resistance genes, including the ATP-binding cassette transporter gene PDR5. PDR5 induction in ⁰ cells requires the presence of the zinc cluster transcription factor Pdr3p. The PDR3 gene is positively autoregulated in ⁰ cells by virtue of the presence of two binding sites for Pdr3p in its promoter. We identify the novel protein Lge1p as a required participant in the ⁰ activation of PDR3 and PDR5 expression. Lge1p is a nuclear protein that has been found to play a role in ubiquitination of histone H2B at Lys¹²³. This ubiquitination requires the presence of the ubiquitin-conjugating enzyme Rad6p and the ubiquitin ligase Bre1p. Interestingly, ⁰ strains lacking Lge1p failed to induce PDR3 transcription, but induction was still seen in rad6, bre1, and H2B-K123R mutant strains. Microarray experiments also confirmed that the pattern of gene expression changes seen in cells lacking Lge1p, Bre1p, or Rad6p or containing the H2B-K123R mutant as the only form of H2B share some overlap but are distinct. These findings provide a strong argument that Lge1p has roles in gene regulation independent of its participation in the Rad6p-dependent ubiquitination of H2B.

Received for publication, July 22, 2004 , and in revised form, October 28, 2004.

^* This work was supported by National Institutes of Health Grant GM49825. 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.

The on-line version of this article (available at http://www.jbc.org) contains Supplemental Table I.

These authors contributed equally to this work.

^¶ Present address: Lab. of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.

^** Present address: Inst. of Biochemistry and Molecular Biology, University of Wroclaw, 50-137 Wroclaw, Poland.

Present address: Dept. of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27705.

^¶¶ To whom correspondence should be addressed: Dept. of Physiology and Biophysics, University of Iowa, 6-530 Bowen Science Bldg., 51 Newton Rd., Iowa City, IA 52242. Tel.: 319-335-7874; Fax: 319-335-7330; E-mail: scott-moye-rowley{at}uiowa.edu.

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