Evidence map›Paper›PMID 22318720›Full record

ArticleThe Journal of biological chemistry2012

Cdc73 subunit of Paf1 complex contains C-terminal Ras-like domain that promotes association of Paf1 complex with chromatin.

Christopher G Amrich, Christopher P Davis, Walter P Rogal, Margaret K Shirra, Annie Heroux, Richard G Gardner, Karen M Arndt, Andrew P VanDemark

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

41 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
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  5. JBMR plus · 2025
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  6. Phenotypic Profiling and Molecular Mechanisms in Hyperparathyroidism-jaw Tumor Syndrome.The Journal of clinical endocrinology and metabolism · 2023
    Article
  7. Article
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  10. Article
  11. The Paf1 complex is required for RNA polymerase II removal in response to DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Biochemical insights into Paf1 complex-induced stimulation of Rad6/Bre1-mediated H2B monoubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Review
  15. Article
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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

8 authors at 3 institutions in 1 country.

Christopher G AmrichDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Christopher P Davis
Walter P Rogal
Margaret K Shirra
Annie Heroux
Richard G Gardner
Karen M Arndt
Andrew P VanDemark
University of Pittsburgh · USBrookhaven National Laboratory · USUniversity of Washington · US

Funding

TRANSCRIPTION FACTOR MUTANTS OF YEASTR01GM052593 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ARNDT, KAREN M · 1995 to 2020
$7.9M
Discovery of ubiquitin ligase substrates - the development of integrated experimeR21RR025787 · NCRR · UNIVERSITY OF WASHINGTON · PI GARDNER, RICHARD GEORGE, RANDOLPH, TIMOTHY W · 2009 to 2010
$616k
NCRR NIH HHS R21 RR025787NCRR NIH HHS R21RR025787NIGMS NIH HHS R01 GM052593NIGMS NIH HHS R01GM52593
6 · The paper itself

Abstract

The conserved Paf1 complex localizes to the coding regions of genes and facilitates multiple processes during transcription elongation, including the regulation of histone modifications. However, the mechanisms that govern Paf1 complex recruitment to active genes are undefined. Here we describe a previously unrecognized domain within the Cdc73 subunit of the Paf1 complex, the Cdc73 C-domain, and demonstrate its importance for Paf1 complex occupancy on transcribed chromatin. Deletion of the C-domain causes phenotypes associated with elongation defects without an apparent loss of complex integrity. Simultaneous mutation of the C-domain and another subunit of the Paf1 complex, Rtf1, causes enhanced mutant phenotypes and loss of histone H3 lysine 36 trimethylation. The crystal structure of the C-domain reveals unexpected similarity to the Ras family of small GTPases. Instead of a deep nucleotide-binding pocket, the C-domain contains a large but comparatively flat surface of highly conserved residues, devoid of ligand. Deletion of the C-domain results in reduced chromatin association for multiple Paf1 complex subunits. We conclude that the Cdc73 C-domain probably constitutes a protein interaction surface that functions with Rtf1 in coupling the Paf1 complex to the RNA polymerase II elongation machinery.

Indexed as

Amino Acid SequenceChromatinConserved SequenceHistonesModels, MolecularMolecular Sequence DataNuclear ProteinsProtein BindingProtein Structure, TertiaryProtein SubunitsProtein Transportras ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscription, GeneticCDC73 protein, S cerevisiaeChromatinHistonesNuclear ProteinsPAF1 protein, S cerevisiaeProtein Subunitsras ProteinsRTF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding Protein

Identifiers

PMID22318720
PMCPMC3322841
OpenAlexW2085639715

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.