Evidence map›Paper›PMID 15180994›Full record

ArticleThe Journal of biological chemistry2004

Effectors of lysine 4 methylation of histone H3 in Saccharomyces cerevisiae are negative regulators of PHO5 and GAL1-10.

Christopher D Carvin, Michael P Kladde

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

36 citing papers in PubMed, 56 citations in OpenAlex.

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  13. The timing is right.Nature structural & molecular biology · 2014
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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

2 authors at 1 institution in 1 country.

Christopher D CarvinDepartment of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843-2128, USA.
Michael P Kladde
Texas A&M University · US

Funding

Regulation of Gene Expression in ChromatinR01CA095525 · NCI · UNIVERSITY OF FLORIDA · PI KLADDE, MICHAEL P · 2003 to 2007
$1.3M
NCI NIH HHS CA95525NCI NIH HHS R01 CA095525
6 · The paper itself

Abstract

Post-translational modifications of histone amino-terminal tails are a key determinant in gene expression. Histone methylation plays a dual role in gene regulation. Methylation of lysine 9 of histone H3 in higher eukaryotes is associated with transcriptionally inactive heterochromatin, whereas H3 lysine 4 methylation correlates with active chromatin. Methylation of lysine 4 of H3 via Set1, a component of the Saccharomyces cerevisiae COMPASS complex, is regulated by the transcriptional elongation Paf1-Rtf1 and histone ubiquitination Rad6-Bre1 complexes, which are required for the expression of a subset of genes. This suggests that lysine 4 methylation of histone H3 may play an activating role in transcription; however, the mechanism of Set1 function remains unclear. We show here that H3 lysine 4 methylation also negatively regulated gene expression, as strains without Set1 showed enhanced expression of PHO5, wherein chromatin structure plays an important transcriptional regulatory role. Di- and trimethylation of H3 lysine 4 was detected at the PHO5 promoter, and a strain expressing a mutant version of histone H3 with lysine 4 changed to arginine, (which cannot be methylated) exhibited PHO5 derepression. Moreover, PHO5 was derepressed in strains that lacked components of either the Paf1-Rtf1 elongation or Rad6-Bre1 histone ubiquitination complexes. Lastly, PHO84 and GAL1-10 transcription was also increased in set1Delta cells. These results suggest that H3 methylation at lysine 4, in conjunction with transcriptional elongation, may function in a negative feedback pathway for basal transcription of some genes, although being a positive effector at others.

Indexed as

Gene Expression RegulationAcid PhosphataseCarrier ProteinsDNA-Binding ProteinsFeedback, PhysiologicalGene DeletionHistone-Lysine N-MethyltransferaseHistonesLysineMethylationMutagenesisNuclear ProteinsPolymerase Chain ReactionProton-Phosphate SymportersRNA, MessengerSaccharomyces cerevisiaeAcid PhosphataseBre1 protein, S cerevisiaeCarrier ProteinsDNA-Binding ProteinsHistone-Lysine N-MethyltransferaseHistonesLysineNuclear ProteinsPAF1 protein, S cerevisiaePHO3 protein, S cerevisiaePHO5 protein, S cerevisiaePHO84 protein, S cerevisiaeProton-Phosphate SymportersRAD6 protein, S cerevisiaeRNA, MessengerRTF1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiaeTATA-Box Binding Proteinthiamine-binding proteinTranscription FactorsUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID15180994
PMCPMC3697737
OpenAlexW1974016204

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.