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J. Biol. Chem., Vol. 279, Issue 24, 25251-25259, June 11, 2004

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Dephosphorylation of RNA Polymerase I by Fcp1p Is Required for Efficient rRNA Synthesis^*

Stephan Fath, Michael S. Kobor¶, Anja Philippi||, Jack Greenblatt**, and Herbert Tschochner||

From the Biochemie-Zentrum Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany, the ^¶Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, the ^||Institut für Biochemie, Mikrobiologie und Genetik, Universität Regensburg, Universitätsstrasse 1, 94034 Regensburg, Germany, and the ^**Banting and Best Dept. of Medical Research and Dept. of Molecular and Medical Genetics, University of Toronto, 112 College Street, Toronto, Ontario M5G 1L6, Canada

Differently phosphorylated forms of RNA polymerase (Pol) II are required to guide the enzyme through the transcription cycle. Here, we show that a phosphorylation/dephosphorylation cycle is also important for RNA polymerase I-dependent synthesis of rRNA precursors. A key component of the Pol II transcription system is Fcp1p, a phosphatase that dephosphorylates the C-terminal domain of the largest Pol II subunit. Fcp1p stimulates transcription elongation and is required for Pol II recycling after transcription termination. We found that Fcp1p is also part of the RNA Pol I transcription apparatus. Fcp1p is required for efficient rDNA transcription in vivo, and also, recombinant Fcp1p stimulates rRNA synthesis both in promoter-dependent and in nonspecific transcription assays in vitro. We demonstrate that Fcp1 activity is not involved in the formation of the initiation-active form of Pol I (the Pol I-Rrn3p complex) and propose that dephosphorylation of Pol I by Fcp1p facilitates chain elongation during rRNA synthesis.

Received for publication, February 20, 2004 , and in revised form, April 5, 2004.

^* This work was supported by funds from the Deutsche Forschungsgemeinschaft (to H. T.) and by grants from the Canadian Institutes of Health Research and the National Cancer Institute of Canada with funds from the Canadian Cancer Society (to J. G.). 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.

Present address: Protein Structure and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Ave., New York, NY 10021.

To whom correspondence should be addressed. Tel.: 49-941-943-2472; Fax: 49-941-943-2474; E-mail: herbert.tschochner{at}vkl.uniregensburg.de.

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