Evidence map›Paper›PMID 23469257›Full record

ArticlePloS one2013

Catalytic and functional roles of conserved amino acids in the SET domain of the S. cerevisiae lysine methyltransferase Set1.

Kelly Williamson, Victoria Schneider, Rachel A Jordan, John E Mueller, Michelle Henderson Pozzi, Mary Bryk

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. 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
0.3field-weighted citation impact, top 37% 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, 23 citations in OpenAlex.

  1. Article
  2. Review
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  4. In silico screening of non-synonymous SNPs in human TUFT1 gene.Journal, genetic engineering & biotechnology · 2023
    Article
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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

6 authors at 3 institutions in 1 country.

Kelly WilliamsonDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, United States of America.
Victoria Schneider
Rachel A Jordan
John E Mueller
Michelle Henderson Pozzi
Mary Bryk
Texas A&M University · USLynntech (United States) · USTexas A&M University System · US

Funding

Role of chromatin structure in regulating gene silencingR01GM070930 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI BRYK, MARY E · 2004 to 2009
$1.4M
NIGMS NIH HHS R01 GM070930NIGMS NIH HHS R01 GM70930
6 · The paper itself

Abstract

In S. cerevisiae, the lysine methyltransferase Set1 is a member of the multiprotein complex COMPASS. Set1 catalyzes mono-, di- and trimethylation of the fourth residue, lysine 4, of histone H3 using methyl groups from S-adenosylmethionine, and requires a subset of COMPASS proteins for this activity. The methylation activity of COMPASS regulates gene expression and chromosome segregation in vivo. To improve understanding of the catalytic mechanism of Set1, single amino acid substitutions were made within the SET domain. These Set1 mutants were evaluated in vivo by determining the levels of K4-methylated H3, assaying the strength of gene silencing at the rDNA and using a genetic assessment of kinetochore function as a proxy for defects in Dam1 methylation. The findings indicate that no single conserved active site base is required for H3K4 methylation by Set1. Instead, our data suggest that a number of aromatic residues in the SET domain contribute to the formation of an active site that facilitates substrate binding and dictates product specificity. Further, the results suggest that the attributes of Set1 required for trimethylation of histone H3 are those required for Pol II gene silencing at the rDNA and kinetochore function.

Indexed as

Gene Expression Regulation, FungalAmino Acid SequenceAmino Acid SubstitutionCatalytic DomainCell Cycle ProteinsConserved SequenceDNA, RibosomalGene SilencingHistone-Lysine N-MethyltransferaseHistonesKinetochoresLysineMicrotubule-Associated ProteinsMolecular Sequence DataMutationRNA, Small InterferingCell Cycle ProteinsDAM1 protein, S cerevisiaeDNA, RibosomalHistone-Lysine N-MethyltransferaseHistonesLysineMicrotubule-Associated ProteinsRNA, Small InterferingSaccharomyces cerevisiae ProteinsS-AdenosylmethionineSET1 protein, S cerevisiae

Identifiers

PMID23469257
PMCPMC3585878
OpenAlexW2089719819

What OpenQuestion holds

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LicenceCC BY
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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.