Evidence map›Paper›PMID 19450536›Full record

ArticleMolecular cell2009

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

Md Sohail Akhtar, Martin Heidemann, Joshua R Tietjen, David W Zhang, Rob D Chapman, Dirk Eick, Aseem Z Ansari

Abstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 195 papers.

0numbers the graph read from it
0cells of the map it votes in
195citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

195 citing papers in PubMed.

  1. Review
  2. Targeting CDKs in the RNAPII transcription cycle.Nature reviews. Drug discovery · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review

135 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Md Sohail AkhtarDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Martin Heidemann
Joshua R Tietjen
David W Zhang
Rob D Chapman
Dirk Eick
Aseem Z Ansari

Funding

Institutional Training in the Genomic SciencesT32HG002760 · NHGRI · UNIVERSITY OF WISCONSIN-MADISON · PI Qiongshi Lu · 2003 to 2026
$17.7M
Modular design of synthetic transcriptional regulatorsR01GM069420 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ANSARI, ASEEM Z · 2006 to 2010
$1.4M
NHGRI NIH HHS 5 T32 HG002760NHGRI NIH HHS T32 HG002760NIGMS NIH HHS R01 GM069420
6 · The paper itself

Abstract

Posttranslational modifications of the carboxy-terminal domain (CTD) of the largest subunit of RNA polymerase II (Pol II) specify a molecular recognition code that is deciphered by proteins involved in RNA biogenesis. The CTD is comprised of a repeating heptapeptide (Y(1)S(2)P(3)T(4)S(5)P(6)S(7)). Recently, phosphorylation of serine 7 was shown to be important for cotranscriptional 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 cotranscriptional engagement of the relevant RNA processing machinery.

Indexed as

RNA Processing, Post-TranscriptionalCyclin-Dependent KinasesHumansPhosphorylationProtein Structure, TertiaryProtein SubunitsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSerineTranscription, GeneticCyclin-Dependent KinasesKin28 protein kinase, S cerevisiaeProtein SubunitsRNA Polymerase IISaccharomyces cerevisiae ProteinsSerine

Identifiers

PMID19450536
PMCPMC2757088

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.