Change search
ReferencesLink to record
Permanent link

Direct link
The Medicago CDKC;1-CYCLINT;1 kinase complex phosphorylates the carboxy-terminal domain of RNA polymerase II and promotes transcription.
Show others and affiliations
2005 (English)In: Plant Journal, ISSN 0960-7412, Vol. 42, no 6, 810-20 p.Article in journal (Refereed) Published
Abstract [en]

The Ms;CDKC;1 kinase is structurally similar to those cyclin-dependent kinases (CDKs) that are not involved directly in cell cycle regulation. The presence of a PITAIRE motif in Ms;CDKC;1 suggests that it interacts with cyclins different from known PSTAIRE/PPTALRE kinase regulatory subunits. Here we demonstrate that a Medicago CYCLINT (CYCT) protein is a specific interactor of Ms;CDKC;1 and the interaction between these two proteins gives rise to an active kinase complex that localizes to the nucleus and phosphorylates the carboxy-terminal YSPTSPS heptapeptide repeat domain (CTD) of the largest subunit of RNA polymerase II in vitro. Mutation of Ser to Ala at position 5 within the heptapeptide repeat abolishes substrate phosphorylation by the Ms;CDKC;1 kinase complex. Furthermore, our data show that addition of the Medicago CDKC;1-CYCT;1 heterodimer completely restored the transcriptional activity of a HeLa nuclear extract depleted of endogeneous CDK9 kinase complexes. Together, these results indicate that the Medicago CDKC;1-CYCT;1 complex is a positive regulator of transcription in plants and has a role similar to the CDK9/cyclin T complex of human positive transcription elongation factor P-TEFb.

Place, publisher, year, edition, pages
2005. Vol. 42, no 6, 810-20 p.
Keyword [en]
Amino Acid Sequence, Cell Nucleus/metabolism, Cyclin-Dependent Kinases/metabolism, Cyclins/metabolism, Gene Expression Regulation; Plant, Hela Cells, Humans, Medicago/*enzymology, Molecular Sequence Data, Multienzyme Complexes/*metabolism, Plant Proteins/*metabolism, RNA Polymerase II/*metabolism, Sequence Alignment, Sequence Homology; Amino Acid, Transcription; Genetic
URN: urn:nbn:se:umu:diva-15843DOI: doi:10.1111/j.1365-313X.2005.02421.xPubMedID: 15941395OAI: diva2:155515
Available from: 2007-08-02 Created: 2007-08-02 Last updated: 2015-04-29Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Bako, Laszlo
By organisation
Department of Plant PhysiologyUmeå Plant Science Centre (UPSC)

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 24 hits
ReferencesLink to record
Permanent link

Direct link