Evidence map›Paper›PMID 22244764›Full record

ArticleStructure (London, England : 1993)2012

Structural basis for molecular interactions involving MRG domains: implications in chromatin biology.

Tao Xie, Richard Graveline, Ganesan Senthil Kumar, Yongbo Zhang, Arvind Krishnan, Gregory David, Ishwar Radhakrishnan

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. PALB2 (partner and localizer of BRCA2).Atlas of genetics and cytogenetics in oncology and haematology · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Structural Basis for Multi-specificity of MRG Domains.Structure (London, England : 1993) · 2015
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. 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

7 authors at 2 institutions in 1 country.

Tao XieDepartment of Molecular Biosciences, Northwestern University, 2205 Tech Drive, Evanston, IL 60208, USA.
Richard Graveline
Ganesan Senthil Kumar
Yongbo Zhang
Arvind Krishnan
Gregory David
Ishwar Radhakrishnan
Northwestern University · USNew York 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
Regulation of Cellular Senescence and Oncogenic Transformation by Sin3B.R01CA148639 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI DAVID, GREGORY · 2011 to 2015
$2.0M
STRUCTURAL BIOL RES: LUNG SURFACTANT PROTEINS, DISTRESSS10RR019071 · NCRR · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 2005 to 2005
$272k
NCI NIH HHS P30 CA060553NCI NIH HHS R01 CA148639NCRR NIH HHS S10 RR019071NIGMS NIH HHS R01 GM064715
6 · The paper itself

Abstract

MRG15 is a member of the mortality family of transcription factors that targets a wide variety of multiprotein complexes involved in transcription regulation, DNA repair, and alternative splicing to chromatin. The structure of the apo-MRG15 MRG domain implicated in interactions with diverse proteins has been described, but not in complex with any of its targets. Here, we structurally and functionally characterize the interaction between MRG15 and Pf1, two constitutively associated subunits of the histone deacetylase-associated Rpd3S/Sin3S corepressor complex. The MRG domain adopts a structure reminiscent of the apo state, whereas the Pf1 MRG-binding domain engages two discrete hydrophobic surfaces on the MRG domain via a bipartite motif comprising an α-helix and a segment in an extended conformation, both of which are critical for high-affinity interactions. Multiple MRG15 interactors share an FxLP motif in the extended segment, but equivalent sequence/helical motifs are not readily evident, implying potential diversity in MRG-recognition mechanisms.

Indexed as

Models, MolecularProtein Structure, TertiaryAmino Acid MotifsAmino Acid SequenceChromatinHumansMolecular Sequence DataProtein BindingSequence AlignmentSin3 Histone Deacetylase and Corepressor ComplexTranscription FactorsChromatinMORF4L1 protein, humanSin3 Histone Deacetylase and Corepressor ComplexTranscription Factors

Identifiers

PMID22244764
PMCPMC3259534
OpenAlexW1970830322

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.