Evidence map›Paper›PMID 17001490›Full record

ArticleMolecular genetics and genomics : MGG2007

Cdk9 is an essential kinase in Drosophila that is required for heat shock gene expression, histone methylation and elongation factor recruitment.

Joel C Eissenberg, Ali Shilatifard, Nikolay Dorokhov, Dorian E Michener

Abstract read
PubMed Publisher
In one paragraph

Article in Molecular genetics and genomics : MGG, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.8field-weighted citation impact, top 17% of its field
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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  9. Review
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  11. RNA polymerase II elongation control.Annual review of biochemistry · 2012
    Review
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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

4 authors at 1 institution in 1 country.

Joel C EissenbergEdward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, 1402 South Grand Blvd, St. Louis, MO 63104, USA. eissenjc@slu.edu
Ali Shilatifard
Nikolay Dorokhov
Dorian E Michener
Saint Louis University · US

Funding

Chromatin Modifications by Histone Ubiquitination and MethylationsR01GM069905 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI SHILATIFARD, ALI · 2004 to 2015
$4.7M
Physiological Role of MLL and ELL Proteins in LeukemiaR01CA089455 · NCI · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI SHILATIFARD, ALI · 2001 to 2015
$3.5M
NCI NIH HHS 2R01CA089455NIGMS NIH HHS 1R01GM069905
6 · The paper itself

Abstract

Phosphorylation of the large RNA Polymerase II subunit C-terminal domain (CTD) is believed to be important in promoter clearance and for recruiting protein factors that function in messenger RNA synthesis and processing. P-TEFb is a protein kinase that targets the (CTD). The goal of this study was to identify chromatin modifications and associations that require P-TEFb activity in vivo. We knocked down the catalytic subunit of P-TEFb, Cdk9, in Drosophila melanogaster using RNA interference. Cdk9 knockdown flies die during metamorphosis. Phosphorylation at serine 2 and serine 5 of the CTD heptad repeat were both dramatically reduced in knockdown larvae. Hsp 70 mRNA induction by heat shock was attenuated in Cdk9 knockdown larvae. Both mono- and trimethylation of histone H3 at lysine 4 were dramatically reduced, suggesting a link between CTD phosphorylation and histone methylation in transcribed chromatin in vivo. Levels of the chromo helicase protein CHD1 were reduced in Cdk9 knockdown chromosomes, suggesting that CHD1 is targeted to chromosomes through P-TEFb-dependent histone methylation. Dimethylation of histone H3 at lysine 36 was significantly reduced in knockdown larvae, implicating CTD phosphorylation in the regulation of this chromatin modification. Binding of the RNA Polymerase II elongation factor ELL was reduced in knockdown chromosomes, suggesting that ELL is recruited to active polymerase via CTD phosphorylation.

Indexed as

Protein Processing, Post-TranslationalAnimalsAnimals, Genetically ModifiedChromosomesCyclin-Dependent Kinase 9DNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsElonginHeat-Shock ProteinsHeat-Shock ResponseHistonesMethylationRNA InterferenceRNA Polymerase IITranscriptional Elongation FactorsASH1 protein, DrosophilaCHD1 protein, DrosophilaCyclin-Dependent Kinase 9DNA-Binding ProteinsDrosophila ProteinsElonginHeat-Shock ProteinsHistonesRNA Polymerase IITranscriptional Elongation FactorsTranscription Factors

Identifiers

PMID17001490
OpenAlexW1980199196

What OpenQuestion holds

Textmetadata
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.