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The structure and substrate specificity of human Cdk12/Cyclin K.
Nat. Commun. 5:3505 (2014)
Phosphorylation of the RNA polymerase II C-terminal domain (CTD) by cyclin-dependent kinases is important for productive transcription. Here we determine the crystal structure of Cdk12/CycK and analyse its requirements for substrate recognition. Active Cdk12/CycK is arranged in an open conformation similar to that of Cdk9/CycT but different from those of cell cycle kinases. Cdk12 contains a C-terminal extension that folds onto the N- and C-terminal lobes thereby contacting the ATP ribose. The interaction is mediated by an HE motif followed by a polybasic cluster that is conserved in transcriptional CDKs. Cdk12/CycK showed the highest activity on a CTD substrate prephosphorylated at position Ser7, whereas the common Lys7 substitution was not recognized. Flavopiridol is most potent towards Cdk12 but was still 10-fold more potent towards Cdk9. T-loop phosphorylation of Cdk12 required coexpression with a Cdk-activating kinase. These results suggest the regulation of Pol II elongation by a relay of transcriptionally active CTD kinases.
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Times Cited
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10.742
2.685
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117
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Rna-polymerase-ii; C-terminal Domain; Capping Enzyme Recruitment; Cyclin-dependent Kinase-9; Ctd Code; P-tefb; Protein-kinases; Fission Yeast; Crystal-structure; In-vivo
Language
english
Publication Year
2014
HGF-reported in Year
2014
ISSN (print) / ISBN
2041-1723
e-ISSN
2041-1723
Journal
Nature Communications
Quellenangaben
Volume: 5,
Article Number: 3505
Publisher
Nature Publishing Group
Publishing Place
London
Reviewing status
Peer reviewed
POF-Topic(s)
30504 - Mechanisms of Genetic and Environmental Influences on Health and Disease
Research field(s)
Immune Response and Infection
PSP Element(s)
G-501490-001
PubMed ID
24662513
WOS ID
WOS:000334302000008
Erfassungsdatum
2014-03-26