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Nucleic Acids Research, 2003, Vol. 31, No. 12 3033-3037
© 2003 Oxford University Press

Yeast Ume6p repressor permits activator binding but restricts TBP binding at the HOP1 promoter

Mitsuhiro Shimizu, Keiko Takahashi, Teresa M. Lamb1, Heisaburo Shindo2 and Aaron P. Mitchell1

Department of Chemistry, Meisei University, Hino, Tokyo 191-8506, Japan, 1 Department of Microbiology and Institute of Cancer Research, Columbia University, New York, NY 10032, USA and 2 School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan

*To whom correspondence should be addressed. Tel: +81 42 591 7483; Fax: +81 42 591 8181; Email: shimizum{at}chem.meisei-u.ac.jp

Ume6p plays essential roles in the regulation of early meiotic genes in Saccharomyces cerevisiae. Ume6p exerts repression via recruitment of the Sin3p-Rpd3p histone deacetylase and Isw2p chromatin remodeling complexes. The transcriptional step that is ultimately inhibited by Ume6p is unknown. Here, in vivo footprinting shows that transcriptional activators Hap1p and Abf1p occupy upstream sites in repressed and derepressed promoters. In contrast, chromatin immunoprecipitation shows that TATA box-binding protein (TBP)- promoter binding is reduced upon repression of HOP1. Fusion of TBP to a zinc cluster DNA binding domain relieves repression at a HOP1 promoter modified to include the zinc cluster target site. We suggest that TBP binding is inhibited through chromatin modification by the Sin3p-Rpd3p and Isw2p complexes recruited by Ume6p.


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