Evidence map›Paper›PMID 26953260›Full record

ArticleJournal of molecular biology2016

Multivalent Interactions by the Set8 Histone Methyltransferase With Its Nucleosome Substrate.

Taverekere S Girish, Robert K McGinty, Song Tan

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

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  15. Molecular basis for chromatin assembly and modification by multiprotein complexes.Protein science : a publication of the Protein Society · 2019
    Review
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  17. Article
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  19. Cryo-electron microscopy of chromatin biology.Acta crystallographica. Section D, Structural biology · 2017
    Review
  20. Review
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 1 institution in 1 country.

Taverekere S GirishCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Robert K McGintyCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
Song TanCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA. Electronic address: sxt30@psu.edu.
Pennsylvania State University · US

Funding

Structural Basis for RCC1 Directed Recruitment of Ran GTPase to ChromatinR01GM088236 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI TAN, SONG · 2009 to 2017
$2.5M
Molecular interactions of histone ubiquitylation enzymes with the nucleosomeR01GM111651 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI TAN, SONG · 2014 to 2017
$1.1M
Damon Runyon Cancer Research Foundation DRG-2107-12NIGMS NIH HHS GM088236NIGMS NIH HHS GM111651NIGMS NIH HHS R01 GM088236NIGMS NIH HHS R01 GM111651
6 · The paper itself

Abstract

Set8 is the only mammalian monomethyltransferase responsible for H4K20me1, a methyl mark critical for genomic integrity of eukaryotic cells. We present here a structural model for how Set8 uses multivalent interactions to bind and methylate the nucleosome based on crystallographic and solution studies of the Set8/nucleosome complex. Our studies indicate that Set8 employs its i-SET and c-SET domains to engage nucleosomal DNA 1 to 1.5 turns from the nucleosomal dyad and in doing so, it positions the SET domain for catalysis with H4 Lys20. Surprisingly, we find that a basic N-terminal extension to the SET domain plays an even more prominent role in nucleosome binding, possibly by making an arginine anchor interaction with the nucleosome H2A/H2B acidic patch. We further show that proliferating cell nuclear antigen and the nucleosome compete for binding to Set8 through this basic extension, suggesting a mechanism for how nucleosome binding protects Set8 from proliferating cell nuclear antigen-dependent degradation during the cell cycle.

Indexed as

Amino Acid SequenceAnimalsArginineCatalytic DomainCell CycleCell Cycle ProteinsGene DeletionGuanine Nucleotide Exchange FactorsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHumansMolecular Sequence DataNuclear ProteinsNucleosomesProtein BindingProteolysisArginineCell Cycle ProteinsGuanine Nucleotide Exchange FactorsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesKMT5A protein, humanNuclear ProteinsNucleosomesRCC1 protein, humanRecombinant Proteinschromatin biologyepigenetichistone modificationsSET domainX-ray crystallography

Identifiers

PMID26953260
PMCPMC5549631
OpenAlexW2292967495

What OpenQuestion holds

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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.