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J. Biol. Chem., Vol. 280, Issue 8, 6455-6462, February 25, 2005

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Two Steps in Maf1-dependent Repression of Transcription by RNA Polymerase III^*

Neelam Desai, JaeHoon Lee, Rajendra Upadhya, Yaya Chu, Robyn D. Moir, and Ian M. Willis

From the Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461

In Saccharomyces cerevisiae, Maf1 is essential for mediating the repression of transcription by RNA polymerase (pol) III in response to diverse cellular conditions. These conditions activate distinct signaling pathways that converge at or above Maf1. Thus, Maf1-dependent repression is thought to involve a common set of downstream inhibitory effects on the pol III machinery. Here we provide support for this view and define two steps in Maf1-dependent transcriptional repression. We show that chlorpromazine (CPZ)-induced repression of pol III transcription is achieved by inhibiting de novo assembly of transcription factor (TF) IIIB onto DNA as well as the recruitment of pol III to preassembled TFIIIB·DNA complexes. Additionally Brf1 was identified as a target of repression in extracts of CPZ-treated cells. Maf1-Brf1 and Maf1-pol III interactions were implicated in the inhibition of TFIIIB·DNA complex assembly and polymerase recruitment by recombinant Maf1. Co-immunoprecipitation experiments confirmed these interactions in yeast extracts and demonstrated that Maf1 does not differentially sequester Brf1 or pol III under repressing conditions. The results suggest that Maf1 functions by a non-stoichiometric mechanism to repress pol III transcription.

Received for publication, November 2, 2004 , and in revised form, November 30, 2004.

^* This work was supported by National Institutes of Health Grants GM60631 and GM42728 (to I. M. W.). 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 Figs. 1 and 2 and the primers used in this study.

Both authors contributed equally to this work.

To whom correspondence should be addressed: Dept. of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Tel.: 718-430-2839; Fax: 718-430-8565; E-mail: willis{at}aecom.yu.edu.

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