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Nucleic Acids Research 2004 32(14):4091-4099; doi:10.1093/nar/gkh732
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Published online 3 August 2004

Nucleic Acids Research, Vol. 32 No. 14 © Oxford University Press 2004; all rights reserved

The chromatin remodeling complex NoRC and TTF-I cooperate in the regulation of the mammalian rRNA genes in vivo

Attila Németh, Ralf Strohner, Ingrid Grummt1 and Gernot Längst*

Adolf Butenandt Institut, Molekularbiologie, Ludwig-Maximilians-Universität München, Schillerstraße 44, D-80336 München, Germany and 1 Division of Molecular Biology of the Cell II, German Cancer Research Center, D-69120 Heidelberg, Germany

* To whom correspondence should be addressed. Tel: +49 89 5996 435; Fax: +49 89 5996 425; Email: laengst{at}lmu.de

Received May 25, 2004; Revised June 23, 2004; Accepted July 12, 2004

The transcription termination factor (TTF)-I is a multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. TTF-I plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. The N-terminal part of TTF-I contains a negative regulatory domain (NRD) that inhibits DNA binding. Here we show that interactions between the NRD and the C-terminal part of TTF-I mask the DNA-binding domain of TTF-I. However, interaction with TIP5, a subunit of the nucleolar chromatin remodeling complex, NoRC, recovers DNA-binding activity. We have mapped the protein domains that mediate the interaction between TTF-I and TIP5. The association of TIP5 with the NRD facilitates DNA binding of TTF-I and leads to the recruitment of NoRC to the rDNA promoter. Thus, TTF-I and NoRC act in concert to silence rDNA transcription.


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