Evidence map›Paper›PMID 25960410›Full record

ArticleStructure (London, England : 1993)2015

Structural Basis for Multi-specificity of MRG Domains.

Tao Xie, Adam M Zmyslowski, Yongbo Zhang, Ishwar Radhakrishnan

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

14 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. MRG15-mediated tethering of PALB2 to unperturbed chromatin protects active genes from genotoxic stress.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  14. 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

4 authors at 1 institution in 2 countries.

Tao XieDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Adam M ZmyslowskiDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Yongbo ZhangDepartment of Chemistry, Northwestern University, Evanston, IL 60208, USA.
Ishwar RadhakrishnanDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA. Electronic address: i-radhakrishnan@northwestern.edu.
Northwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
Structural Biology of the Sin3 Corepressor ComplexR01GM064715 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 2002 to 2011
$2.4M
STRUCTURAL BIOL RES: LUNG SURFACTANT PROTEINS, DISTRESSS10RR019071 · NCRR · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 2005 to 2005
$272k
600 MHz NMR Instrument Upgrade at Northwestern UniversityS10OD012016 · OD · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 2012 to 2012
$267k
NCI NIH HHS P30 CA060553NCRR NIH HHS S10 RR019071NIGMS NIH HHS R01 GM064715NIGMS NIH HHS R01GM64715NIH HHS S10 OD012016
6 · The paper itself

Abstract

Chromatin-binding proteins play vital roles in the assembly and recruitment of multi-subunit complexes harboring effector proteins to specific genomic loci. MRG15, a chromodomain-containing chromatin-binding protein, recruits diverse chromatin-associated complexes that regulate gene transcription, DNA repair, and RNA splicing. Previous studies with Pf1, another chromatin-binding subunit of the Sin3S/Rpd3S histone deacetylase complex, defined the sequence and structural requirements for interactions with the MRG15 MRG domain, a common target of diverse subunits in the aforementioned complexes. We now show that MRGBP, a member of the Tip60/NuA4 histone acetyltransferase complex, engages the same two surfaces of the MRG domain as Pf1. High-affinity interactions occur via a bipartite structural motif including an FxLP sequence motif. MRGBP shares little sequence and structural similarity with Pf1, yet targets similar pockets on the surface of the MRG domain, mimicking Pf1 in its interactions. Our studies shed light onto how MRG domains have evolved to bind diverse targets.

Indexed as

Evolution, MolecularModels, MolecularAmino Acid SequenceBinding SitesCarrier ProteinsHistone AcetyltransferasesHistone DeacetylasesHumansMolecular Sequence DataMultiprotein ComplexesNuclear Magnetic Resonance, BiomolecularNuclear ProteinsProtein BindingProtein Structure, TertiarySequence AlignmentTranscription FactorsCarrier ProteinsHistone AcetyltransferasesHistone DeacetylasesMORF4L1 protein, humanMRGBP protein, humanMultiprotein ComplexesNuclear ProteinsTranscription Factors

Identifiers

PMID25960410
PMCPMC4456287
OpenAlexW1894026505

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.