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TFIIH kinase places bivalent marks on the carboxyl-terminal domain of RNA polymerase II

IR@CDRI: CSIR-Central Drug Research Institute, Lucknow

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Field Value
 
Creator Akhtar, M S
Heidemann, Martin
Tietjen, Joshua
Zhang, David
Chapman, R D
Eick, Dirk
Ansari, A Z
 
Date 2010-12-11T07:26:19Z
2010-12-11T07:26:19Z
2009
 
Identifier Molecular Cell 34(3) 2009, 387-393
http://hdl.handle.net/123456789/643
 
Description Post-translational modifications of the carboxyl-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) specify a code that is deciphered by proteins involved in RNA biogenesis. The CTD is comprised of a repeating heptapeptide (Y1S2P3T4S5P6S7). Recently, phosphorylation of Serine7 was shown to be important for co-transcriptional processing of two snRNAs in mammalian cells. Here, we report that Kin28/Cdk7, a subunit of the evolutionarily conserved TFIIH complex, is a Ser7 kinase. The ability of Kin28/Cdk7 to phosphorylate Ser7 is particularly surprising because this kinase functions at promoters of protein-coding genes, rather than being restricted to promoter-distal regions of snRNA genes. Kin28/Cdk7 is also known to phosphorylate Ser5 residues of the CTD at gene promoters. Taken together, our results implicate the TFIIH kinase in placing bivalent Ser5 and Ser7 marks early in gene transcription. These bivalent CTD marks, in concert with cues within nascent transcripts, specify the co-transcriptional engagement of the relevant RNA processing machinery.
 
Format 125450 bytes
application/pdf
 
Language en
 
Subject In vitro kinase
TFIIH
ChIP-chip analysis
 
Title TFIIH kinase places bivalent marks on the carboxyl-terminal domain of RNA polymerase II
 
Type Article