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Originally published In Press as doi:10.1074/jbc.M205192200 on July 22, 2002

J. Biol. Chem., Vol. 277, Issue 39, 36061-36067, September 27, 2002
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FCP1 Phosphorylation by Casein Kinase 2 Enhances Binding to TFIIF and RNA Polymerase II Carboxyl-terminal Domain Phosphatase Activity*

Benoît Palancade, Marie-Françoise Dubois, and Olivier BensaudeDagger

From the UMR 8541 CNRS, Génétique Moléculaire, Ecole Normale Supérieure, 46 rue d'Ulm, 75230 Paris Cedex 05, France

Dephosphorylation of RNA polymerase II carboxyl-terminal domain (CTD) is required to resume sequential transcription cycles. FCP1 (TFIIF-dependent CTD phosphatase 1) is the only known phosphatase targeting RNAP II CTD. Here we show that in Xenopus laevis cells, xFCP1 is a phosphoprotein. On the basis of biochemical fractionation and drug sensitivity, casein kinase 2 (CK2) is shown to be the major kinase involved in xFCP1 phosphorylation in X. laevis egg extracts. CK2 phosphorylates xFCP1 mainly at a cluster of serines centered on Ser457. CK2-dependent phosphorylation enhances 4-fold the CTD phosphatase activity of FCP1 and its binding to the RAP74 subunit of general transcription factor TFIIF. These findings unravel a new mechanism regulating CTD phosphorylation and hence class II gene transcription.

* This work was supported by grants from Ligue Nationale Contre le Cancer, Agence Nationale de Recherche sur le SIDA, and Association pour la Recherche sur le Cancer.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 33-1-44-32-34- 10; Fax: 33-1-44-32-39-41; E-mail: bensaude@wotan.ens.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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