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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 30 Sept 2003

Byrd Kristin Nastase, Shearn Allen

Abstract excerpt

Covalent modifications of histone tails modulate gene expression via chromatin organization. As examples, methylation of lysine 9 residues of histone H3 (H3) (H3-K9) is believed to repress transcription by compacting chromatin, whereas methylation of lysine 4 residues of H3 (H3-K4) is believed to activate transcription by relaxing chromatin. The Drosophila trithorax group protein absent, small, or homeotic discs...

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Identifiers

PMID: 13679578
DOI: 10.1073/pnas.1933593100
PMCID: PMC208793

Genes

SET

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3.PMID 13679578Read ↗

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Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1.Semantic proximity Read ↗

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Functional dissection of the ash2 and ash1 transcriptomes provides insights into the transcriptional basis of wing phenotypes and reveals conserved protein interactions.Semantic proximity Read ↗

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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.Semantic proximity Read ↗

A unique histone 3 lysine 14 chromatin signature underlies tissue-specific gene regulation.Semantic proximity Read ↗

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