Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism.

doi:10.1016/s0960-9822(01)00652-2

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Article

Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism.

Current biology : CB - 22 Jan 2002

Bryk Mary, Briggs Scott D, Strahl Brian D, Curcio M Joan, Allis C David, Winston Fred

Abstract excerpt

Several types of histone modifications have been shown to control transcription. Recent evidence suggests that specific combinations of these modifications determine particular transcription patterns. The histone modifications most recently shown to play critical roles in transcription are arginine-specific and lysine-specific methylation. Lysine-specific histone methyltransferases all contain a SET domain, a...

Topics

Acetylation
DNA Methylation
DNA, Ribosomal
DNA-Binding Proteins
Drosophila Proteins
Fungal Proteins
Gene Silencing
Histone Deacetylases
Histone-Lysine N-Methyltransferase
Histones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Silent Information Regulator Proteins, Saccharomyces cerevisiae

Sirtuin 2

Sirtuins

Trans-Activators

Transcription Factors

Source

Open in PubMed

Identifiers

PMID: 11818070
DOI: 10.1016/s0960-9822(01)00652-2

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Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-11818070-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism.PMID 11818070Read ↗

Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae.Semantic proximity Read ↗

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

A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3.Semantic proximity Read ↗

Simultaneous mutation of methylated lysine residues in histone H3 causes enhanced gene silencing, cell cycle defects, and cell lethality in Saccharomyces cerevisiae.Semantic proximity Read ↗

Set2-catalyzed methylation of histone H3 represses basal expression of GAL4 in Saccharomyces cerevisiae.Semantic proximity Read ↗

Histone trimethylation by Set1 is coordinated by the RRM, autoinhibitory, and catalytic domains.Semantic proximity Read ↗

SET1, a yeast member of the trithorax family, functions in transcriptional silencing and diverse cellular processes.Semantic proximity Read ↗

Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association.Semantic proximity Read ↗

Methylation of histone H3 by COMPASS requires ubiquitination of histone H2B by Rad6.Semantic proximity Read ↗

H3K4 Methylation Dependent and Independent Chromatin Regulation by JHD2 and SET1 in Budding Yeast.Semantic proximity Read ↗

A region of the nucleosome required for multiple types of transcriptional silencing in Saccharomyces cerevisiae.Semantic proximity Read ↗

ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3.Semantic proximity Read ↗

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