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Molecular and Cellular Biology, January 2003, p. 195-205, Vol. 23, No. 1
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.1.195-205.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

An Rpb4/Rpb7-Like Complex in Yeast RNA Polymerase III Contains the Orthologue of Mammalian CGRP-RCP

Magali Siaut,1 Cécile Zaros,1 Emilie Levivier,2 Maria-Laura Ferri,1,1 Magali Court,3 Michel Werner,1 Isabelle Callebaut,2 Pierre Thuriaux,1 André Sentenac,1 and Christine Conesa1*

Service de Biochimie et de Génétique Moléculaire, CEA/Saclay, F-91191 Gif sur Yvette Cedex,1 Systèmes Moléculaires et Biologie Structurale, LMCP/CNRS UMR 7590, Universités Paris 6/7, F-75252 Paris Cedex 05,2 DRDC/Chimie des protéines, CEA de Grenoble, 38054 Grenoble, France3

Received 6 June 2002/ Returned for modification 6 August 2002/ Accepted 30 September 2002

The essential C17 subunit of yeast RNA polymerase (Pol) III interacts with Brf1, a component of TFIIIB, suggesting a role for C17 in the initiation step of transcription. The protein sequence of C17 (encoded by RPC17) is conserved from yeasts to humans. However, mammalian homologues of C17 (named CGRP-RCP) are known to be involved in a signal transduction pathway related to G protein-coupled receptors, not in transcription. In the present work, we first establish that human CGRP-RCP is the genuine orthologue of C17. CGRP-RCP was found to functionally replace C17 in {Delta}rpc17 yeast cells; the purified mutant Pol III contained CGRP-RCP and had a decreased specific activity but initiated faithfully. Furthermore, CGRP-RCP was identified by mass spectrometry in a highly purified human Pol III preparation. These results suggest that CGRP-RCP has a dual function in mammals. Next, we demonstrate by genetic and biochemical approaches that C17 forms with C25 (encoded by RPC25) a heterodimer akin to Rpb4/Rpb7 in Pol II. C17 and C25 were found to interact genetically in suppression screens and physically in coimmunopurification and two-hybrid experiments. Sequence analysis and molecular modeling indicated that the C17/C25 heterodimer likely adopts a structure similar to that of the archaeal RpoE/RpoF counterpart of the Rpb4/Rpb7 complex. These RNA polymerase subunits appear to have evolved to meet the distinct requirements of the multiple forms of RNA polymerases.

* Corresponding author. Mailing address: Service de Biochimie et de Génétique Moléculaire, CEA/Saclay, F-91191 Gif-sur-Yvette Cedex, France. Phone: 33 1 69 08 37 96. Fax: 33 1 69 08 47 12. E-mail: conesa{at}matthieu.saclay.cea.fr.

{dagger} Present address: Laboratoire de Biochimie, Ecole Polytechnique, F-91128 Palaiseau Cedex, France.

Molecular and Cellular Biology, January 2003, p. 195-205, Vol. 23, No. 1
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.1.195-205.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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