Evidence map›Paper›PMID 20943666›Full record

ArticleThe Journal of biological chemistry2010

Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4.

Stanley A Moore, Yurdagul Ferhatoglu, Yunhua Jia, Rami A Al-Jiab, Maxwell J Scott

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
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  5. Histone Readers and Their Roles in Cancer.Cancer treatment and research · 2023
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  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. MRG15 is required for pre-mRNA splicing and spermatogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Stanley A MooreDepartment of Biochemistry, University of Saskatchewan, Saskatoon, SK S7N 5E5, Canada. stan.moore@usask.ca
Yurdagul Ferhatoglu
Yunhua Jia
Rami A Al-Jiab
Maxwell J Scott
University of Saskatchewan · CAMassey University · NZ

Funding

Canadian Institutes of Health Research MOP 79377
6 · The paper itself

Abstract

We have determined the human male specific lethal 3 (hMSL3) chromo-barrel domain structure by x-ray crystallography to a resolution of 2.5 Å (r = 0.226, R(free) = 0.270). hMSL3 contains a canonical methyllysine binding pocket made up of residues Tyr-31, Phe-56, Trp-59, and Trp-63. A six-residue insertion between strands β(1) and β(2) of the hMSL3 chromo-barrel domain directs the side chain of Glu-21 into the methyllysine binding pocket where it hydrogen bonds to the NH group of a bound cyclohexylamino ethanesulfonate buffer molecule, likely mimicking interactions with a histone tail dimethyllysine residue. In vitro binding studies revealed that both the human and Drosophila MSL3 chromo-barrel domains bind preferentially to peptides representing the mono or dimethyl isoform of lysine 20 on the histone H4 N-terminal tail (H4K20Me(1) or H4K20Me(2)). Mutation of Tyr-31 to Ala in the hMSL3 methyllysine-binding cage resulted in weaker in vitro binding to H4K20Me(1). The same mutation in the msl3 gene compromised male survival in Drosophila. Combined mutation of Glu-21 and Pro-22 to Ala in hMSL3 resulted in slightly weaker in vitro binding to H4K20Me(1), but the corresponding msl3 mutation had no effect on male survival in Drosophila. We propose MSL3 plays an important role in targeting the male specific lethal complex to chromatin in both humans and flies by binding to H4K20Me(1). Binding studies on the related dMRG15 chromo-barrel domain revealed that MRG15 prefers binding to H4K20Me(3).

Indexed as

Drosophila ProteinsHistonesNuclear ProteinsTranscription FactorsAmino Acid SubstitutionAnimalsAnimals, Genetically ModifiedBinding SitesChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDrosophila melanogasterFemaleHumansMaleMutation, MissenseProtein BindingChromosomal Proteins, Non-HistoneDNA-Binding ProteinsDrosophila ProteinsHistonesmsl-3 protein, DrosophilaMSL3 protein, humanNuclear ProteinsTranscription Factors

Identifiers

PMID20943666
PMCPMC3003388
OpenAlexW2153827414

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.