Cdk11-cyclinL controls the assembly of the RNA polymerase II mediator complex.
| Autor: | Drogat J; Namur Research College (NARC), The University of Namur, Namur 5000 Belgium., Migeot V, Mommaerts E, Mullier C, Dieu M, van Bakel H, Hermand D |
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| Jazyk: | angličtina |
| Zdroj: | Cell reports [Cell Rep] 2012 Nov 29; Vol. 2 (5), pp. 1068-76. Date of Electronic Publication: 2012 Nov 01. |
| DOI: | 10.1016/j.celrep.2012.09.027 |
| Abstrakt: | The large Mediator (L-Mediator) is a general coactivator of RNA polymerase II transcription and is formed by the reversible association of the small Mediator (S-Mediator) and the kinase-module-harboring Cdk8. It is not known how the kinase module association/dissociation is regulated. We describe the fission yeast Cdk11-L-type cyclin pombe (Lcp1) complex and show that its inactivation alters the global expression profile in a manner very similar to that of mutations of the kinase module. Cdk11 is broadly distributed onto chromatin and phosphorylates the Med27 and Med4 Mediator subunits on conserved residues. The association of the kinase module and the S-Mediator is strongly decreased by the inactivation of either Cdk11 or the mutation of its target residues on the Mediator. These results show that Cdk11-Lcp1 regulates the association of the kinase module and the S-Mediator to form the L-Mediator complex. (Copyright © 2012 The Authors. Published by Elsevier Inc. All rights reserved.) |
| Databáze: | MEDLINE |
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