Evidence map›Paper›PMID 21443952›Full record

ArticleMethods (San Diego, Calif.)2011

Nucleosomal H2B ubiquitylation with purified factors.

Jaehoon Kim, Robert G Roeder

Open access · greenAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

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  13. Spinal RNF20-Mediated Histone H2B Monoubiquitylation Regulates mGluR5 Transcription for Neuropathic Allodynia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
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  17. Preparation and analysis of positioned mononucleosomes.Methods in molecular biology (Clifton, N.J.) · 2015
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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

2 authors at 1 institution in 1 country.

Jaehoon KimLaboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
Robert G Roeder
Rockefeller University · US

Funding

Nuclear Receptor Coactivator Functions and MechanismsR01DK071900 · NIDDK · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 2005 to 2015
$5.9M
Mechanisms of p53 target gene activation in DNA damage responsesR01CA129325 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 2007 to 2011
$4.0M
NCI NIH HHS CA129325NCI NIH HHS R01 CA129325NIDDK NIH HHS DK071900NIDDK NIH HHS R01 DK071900
6 · The paper itself

Abstract

Diverse histone modifications play important roles in transcriptional regulation throughout eukaryotes, and recent studies have implicated histone H2B ubiquitylation in active transcription. The necessity of at least three enzymes (E1-E3), as well as ongoing transcription events, for efficient H2B ubiquitylation complicates mechanistic studies of H2B ubiquitylation relative to other histone modifications. Here we describe experimental protocols for preparation of human H2B ubiquitylation factors, ubiquitylation substrates and transcription factors, as well as the use of these factors to establish H2B ubiquitylation mechanisms during transcription. The methods include reliable protein interaction and E3 ubiquitylation assays that can be widely applied to confirm cognate E2-E3 pairs in other protein ubiquitylation systems, optimized in vitro ubiquitylation assays for various histone substrates, and a transcription-coupled H2B ubiquitylation assay in a highly purified transcription system. These comprehensive analyses have revealed (i) that RAD6 serves as the cognate E2 for the BRE1 complex in human cells, as previously established in yeast, (ii) that RAD6, through direct interaction with the BRE1 complex, ubiquitylates chromatinized H2B at lysine 120 and (iii) that PAF1 complex-mediated transcription is required for efficient H2B ubiquitylation. This experimental system permits detailed mechanistic analyses of H2B ubiquitylation during transcription by providing information concerning both precise enzyme functions and physical interactions between the transcription and histone modification machineries.

Indexed as

UbiquitinationAnimalsCell-Free SystemChromatinChromatin Assembly and DisassemblyCloning, MolecularDrosophila ProteinsEnzyme AssaysEscherichia coliGenetic VectorsHistone ChaperonesHistonesHumansNucleosomesProtein BindingRecombinant Fusion ProteinsChromatinDrosophila ProteinsHistone ChaperonesHistonesNucleosomesRecombinant Fusion ProteinsTranscription FactorsUbiquitin-Conjugating EnzymesXenopus Proteins

Identifiers

PMID21443952
PMCPMC3118980
OpenAlexW2092038358

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.