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Originally published In Press as doi:10.1074/jbc.M010162200 on December 15, 2000

J. Biol. Chem., Vol. 276, Issue 11, 8005-8013, March 16, 2001
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Activation of the Cyclin-dependent Kinase CTDK-I Requires the Heterodimerization of Two Unstable Subunits*

Guillaume HautbergueDagger and Valérie Goguel§

From the Service de Biochimie et Génétique Moléculaire, CEA/Saclay, Gif sur Yvette 91191, France

RNA polymerase II CTD kinases are key elements in the control of mRNA synthesis. They constitute a family of cyclin-dependent kinases activated by C-type cyclins. Unlike most cyclin-dependent kinase complexes, which are composed of a catalytic and a regulatory subunit, the yeast CTD kinase I complex contains three specific subunits: a kinase subunit (Ctk1), a cyclin subunit (Ctk2), and a third subunit (Ctk3) of unknown function that does not exhibit any similarity to known proteins. Like the Ctk2 cyclin that is regulated at the level of protein turnover, Ctk3 is an unstable protein processed through a ubiquitin-proteasome pathway. Interestingly, Ctk2 and Ctk3 physical interaction is required to protect both subunits from degradation, pointing to a new mechanism for cyclin turnover regulation. We also show that Ctk2 and Ctk3 can each interact independently with the kinase. However, despite the formation of CDK/cyclin complexes in vitro, the Ctk2 cyclin is unable to activate its CDK: both Ctk2 and Ctk3 are required for Ctk1 CTD kinase activation. The different specific features governing CTDK-I regulation probably reflect requirement for the transcriptional response to multiple growth conditions.

* 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 Supported by a French Ministère de la Recherche et des Technologies fellowship and by the Association pour la Recherche contre le Cancer.

§ To whom correspondence should be addressed: Tel.: 33-1-6908-9921; Fax: 33-1-6908-4712; E-mail: goguel@jonas.saclay.cea.fr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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