Evidence map›Paper›PMID 32414844›Full record

ArticleThe Journal of biological chemistry2020

Binding and allosteric transmission of histone H3 Lys-4 trimethylation to the recombinase RAG-1 are separable functions of the RAG-2 plant homeodomain finger.

Meiling R May, John T Bettridge, Stephen Desiderio

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 96% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Article
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

3 authors at 2 institutions in 1 country.

Meiling R MayDepartment of Molecular Biology and Genetics and Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
John T BettridgeDepartment of Molecular Biology and Genetics and Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Stephen DesiderioDepartment of Molecular Biology and Genetics and Institute for Cell Engineering, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA; Division of Hematology, Department of Medicine, The Johns Hopkins University School of Medicine, Baltimore, Maryland, USA. Electronic address: sdesider@jhmi.edu.
Johns Hopkins University · USJohns Hopkins Medicine · US

Funding

BIOCHEMISTRY, CELLULAR AND MOLECULAR BIOLOGY PROGRAMT32GM007445 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI GREEN, RACHEL · 1985 to 2021
$24.1M
Temporal and Spatial Control of V(D)J RecombinationR01CA160256 · NCI · JOHNS HOPKINS UNIVERSITY · PI DESIDERIO, STEPHEN V · 2012 to 2016
$1.8M
NCI NIH HHS R01 CA160256NIGMS NIH HHS T32 GM007445
6 · The paper itself

Abstract

V(D)J recombination is initiated by the recombination-activating gene protein (RAG) recombinase, consisting of RAG-1 and RAG-2 subunits. The susceptibility of gene segments to cleavage by RAG is associated with gene transcription and with epigenetic marks characteristic of active chromatin, including histone H3 trimethylated at lysine 4 (H3K4me3). Binding of H3K4me3 by a plant homeodomain (PHD) in RAG-2 induces conformational changes in RAG-1, allosterically stimulating substrate binding and catalysis. To better understand the path of allostery from the RAG-2 PHD finger to RAG-1, here we employed phylogenetic substitution. We observed that a chimeric RAG-2 protein in which the mouse PHD finger is replaced by the corresponding domain from the shark

Indexed as

Allosteric RegulationAnimalsBinding SitesChromatinDNA-Binding ProteinsHistonesHomeodomain ProteinsLysineMethylationMicePhylogenyProtein BindingRecombinasesSharksSubstrate SpecificityVDJ RecombinasesChromatinDNA-Binding Proteinshistone H3 trimethyl Lys4HistonesHomeodomain ProteinsLysineRAG-1 proteinRecombinasesVDJ RecombinasesV(D)J recombination activating protein 2allosteric regulationconformational changeDNA recombinationepigeneticsH3K4me3histone methylationPHD fingerrecombination-activating (RAG) recombinaseV(D)J rearrangement

Identifiers

PMID32414844
PMCPMC7335790
OpenAlexW3025964037

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.