Evidence map›Paper›PMID 27840029›Full record

ArticleMolecular cell2016

The Histone Modification Domain of Paf1 Complex Subunit Rtf1 Directly Stimulates H2B Ubiquitylation through an Interaction with Rad6.

S Branden Van Oss, Margaret K Shirra, Alain R Bataille, Adam D Wier, Kuangyu Yen, Vinesh Vinayachandran, In-Ja L Byeon, Christine E Cucinotta, Annie Héroux, Jongcheol Jeon and 4 more

Open access · greenAbstract read
In one paragraph

Article in Molecular cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 126 citations in OpenAlex.

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  20. Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024
    Review

14 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

14 authors at 5 institutions in 3 countries.

S Branden Van OssDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Margaret K ShirraDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Alain R BatailleCenter for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, PA 16802, USA.
Adam D WierDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Kuangyu YenCenter for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, PA 16802, USA; Department of Developmental Biology, Southern Medical University, Guangzhou 510515, China.
Vinesh VinayachandranCenter for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, PA 16802, USA.
In-Ja L ByeonDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15260, USA.
Christine E CucinottaDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Annie HérouxDepartment of Biology, Brookhaven National Laboratory, Upton, NY 11973, USA.
Jongcheol JeonDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
Jaehoon KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, South Korea.
Andrew P VanDemarkDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
B Franklin PughCenter for Eukaryotic Gene Regulation, Pennsylvania State University, University Park, PA 16802, USA.
Karen M ArndtDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA. Electronic address: arndt@pitt.edu.
University of Pittsburgh · USPennsylvania State University · USKorea Advanced Institute of Science and Technology · KRBrookhaven National Laboratory · USSouthern Medical University · CN

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CALERO, GUILLERMO ALBERTO · 2007 to 2018
$48.1M
TRANSCRIPTION FACTOR MUTANTS OF YEASTR01GM052593 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ARNDT, KAREN M · 1995 to 2020
$7.9M
High Resolution Mapping of Function Elements in the Yeast GenomeR01HG004160 · NHGRI · PENNSYLVANIA STATE UNIVERSITY, THE · PI PUGH, B FRANKLIN · 2007 to 2022
$5.3M
High Resolution Mapping of Functional Elements in the Yeast GenomeR56HG004160 · NHGRI · PENNSYLVANIA STATE UNIVERSITY, THE · PI PUGH, B FRANKLIN · 2017 to 2017
$300k
NHGRI NIH HHS R01 HG004160NHGRI NIH HHS R56 HG004160NIGMS NIH HHS P50 GM082251NIGMS NIH HHS R01 GM052593
6 · The paper itself

Abstract

The five-subunit yeast Paf1 complex (Paf1C) regulates all stages of transcription and is critical for the monoubiquitylation of histone H2B (H2Bub), a modification that broadly influences chromatin structure and eukaryotic transcription. Here, we show that the histone modification domain (HMD) of Paf1C subunit Rtf1 directly interacts with the ubiquitin conjugase Rad6 and stimulates H2Bub independently of transcription. We present the crystal structure of the Rtf1 HMD and use site-specific, in vivo crosslinking to identify a conserved Rad6 interaction surface. Utilizing ChIP-exo analysis, we define the localization patterns of the H2Bub machinery at high resolution and demonstrate the importance of Paf1C in targeting the Rtf1 HMD, and thereby H2Bub, to its appropriate genomic locations. Finally, we observe HMD-dependent stimulation of H2Bub in a transcription-free, reconstituted in vitro system. Taken together, our results argue for an active role for Paf1C in promoting H2Bub and ensuring its proper localization in vivo.

Indexed as

Gene Expression Regulation, FungalAmino Acid MotifsBinding SitesChromosomal Proteins, Non-HistoneCross-Linking ReagentsCrystallography, X-RayFormaldehydeHistonesModels, MolecularNuclear ProteinsProtein BindingProtein Conformation, alpha-HelicalProtein Interaction Domains and MotifsRecombinant ProteinsRNA Polymerase IISaccharomyces cerevisiaeBre1 protein, S cerevisiaeChromosomal Proteins, Non-HistoneCross-Linking ReagentsFormaldehydeHistonesNuclear ProteinsRAD6 protein, S cerevisiaeRecombinant ProteinsRNA Polymerase IIRTF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSPT4 protein, S cerevisiaeSPT5 transcriptional elongation factorTATA-Box Binding ProteinTranscriptional Elongation FactorsUbiquitin-Conjugating EnzymesBre1chromatinH2B ubiquitylationhistone modificationsPaf1 complexRad6RNA Polymerase IIRtf1transcription elongation

Identifiers

PMID27840029
PMCPMC5131541
OpenAlexW2553142899

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.