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Nucleic Acids Research 2005 33(11):3582-3590; doi:10.1093/nar/gki672
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Published online 24 June 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Distinct regions of RPB11 are required for heterodimerization with RPB3 in human and yeast RNA polymerase II

Wagane J. Benga, Sylvie Grandemange1, George V. Shpakovski2, Elena K. Shematorova2, Claude Kedinger and Marc Vigneron*

Unité Mixte de Recherche 7100 CNRS–Université Louis Pasteur, Ecole Supérieure de Biotechnologie de Strasbourg Boulevard Sébastien Brandt, BP 10413, 67412 Illkirch Cedex, France 1Génétique des Maladies Inflammatoires, Institut de Génétique Humaine UPR 1142 CNRS. 141, rue de la Cardonille, 34396 Montpellier Cedex 5, France 2Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences ul. Miklukho-Maklaya 16/10, GSP-7, 117997 Moscow, Russia

*To whom correspondence should be addressed. Tel: +33 3 90 24 47 82; Fax: +33 3 90 24 47 70; Email: marc.vigneron{at}esbs.u-strasbg.fr

Received April 20, 2005. Revised June 7, 2005. Accepted June 7, 2005.

In Saccharomyces cerevisiae, RNA polymerase II assembly is probably initiated by the formation of the RPB3–RPB11 heterodimer. RPB3 is encoded by a single copy gene in the yeast, mouse and human genomes. The RPB11 gene is also unique in yeast and mouse, but in humans a gene family has been identified that potentially encodes several RPB11 proteins differing mainly in their C-terminal regions. We compared the abilities of both yeast and human proteins to heterodimerize. We show that the yeast RPB3/RPB11 heterodimer critically depends on the presence of the C-terminal region of RPB11. In contrast, the human heterodimer tolerates significant changes in RPB11 C-terminus, allowing two human RPB11 variants to heterodimerize with the same efficiency with RPB3. In keeping with this observation, the interactions between the conserved N-terminal ‘{alpha}-motifs’ is much more important for heterodimerization of the human subunits than for those in yeast. These data indicate that the heterodimerization interfaces have been modified during the course of evolution to allow a recent diversification of the human RPB11 subunits that remains compatible with heterodimerization with RPB3.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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