Evidence map›Paper›PMID 11839796›Full record

ArticleMolecular and cellular biology2002

Kin28 is found within TFIIH and a Kin28-Ccl1-Tfb3 trimer complex with differential sensitivities to T-loop phosphorylation.

Michael-Christopher Keogh, Eun-Jung Cho, Vladimir Podolny, Stephen Buratowski

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In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

44 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  7. Structural basis for CDK7 activation by MAT1 and Cyclin H.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. The cryoelectron microscopy structure of the human CDK-activating kinase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
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  12. Axonal neuropathy with neuromyotonia: there is a HINT.Brain : a journal of neurology · 2017
    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 2 countries.

Michael-Christopher KeoghDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Eun-Jung Cho
Vladimir Podolny
Stephen Buratowski
Harvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Basal transcription factor TFIIH phosphorylates the RNA polymerase II (RNApII) carboxy-terminal domain (CTD) within the transcription initiation complex. The catalytic kinase subunit of TFIIH is a member of the cyclin-dependent kinase (Cdk) family, designated Kin28 in Saccharomyces cerevisiae and Cdk7 in higher eukaryotes. Together with TFIIH subunits cyclin H and Mat1, Cdk7 kinase is also found in a trimer complex known as Cdk activating kinase (CAK). A yeast trimer complex has not previously been identified, although a Kin28-Ccl1 dimer called TFIIK has been isolated as a breakdown product of TFIIH. Here we show that a trimeric complex of Kin28-Ccl1-Tfb3 exists in yeast extracts. Several Kin28 point mutants that are defective in CTD phosphorylation were created. Consistent with earlier studies, these mutants have no transcriptional defect in vitro. Like other Cdks, Kin28 is activated by phosphorylation on T162 of the T loop. Kin28 T162 mutants have no growth defects alone but do demonstrate synthetic phenotypes when combined with mutant versions of the cyclin partner, Ccl1. Surprisingly, these phosphorylation site mutants appear to destabilize the association of the cyclin subunit within the context of TFIIH but not within the trimer complex.

Indexed as

Cyclin-Dependent KinasesTATA-Binding Protein Associated FactorsTranscription Factors, TFIITranscription Factor TFIIDDNA RepairMutagenesis, Site-DirectedPhosphorylationProtein ConformationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityTranscription FactorsTranscription Factor TFIIHTranscription, GeneticCCL1 protein, S cerevisiaeCyclin-Dependent KinasesKin28 protein kinase, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsTAF6 protein, S cerevisiaeTATA-Binding Protein Associated FactorsTFB3 protein, S cerevisiaeTranscription FactorsTranscription Factors, TFIITranscription Factor TFIIDTranscription Factor TFIIH

Identifiers

PMID11839796
PMCPMC134711
OpenAlexW2145049521

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.