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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 8 Jan 2002

Nagy Peter L, Griesenbeck Joachim, Kornberg Roger D, Cleary Michael L

Abstract excerpt

Histone methylation has emerged as an important mechanism for regulating the transcriptional accessibility of chromatin. Several methyltransferases have been shown to target histone amino-terminal tails and mark nucleosomes associated with either euchromatic or heterochromatic states. However, the biochemical machinery responsible for regulating histone methylation and integrating it with other cellular events...

Topics

Animals
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Chromatin
DNA-Binding Proteins
Dosage Compensation, Genetic
Drosophila Proteins
Drosophila melanogaster
Electrophoresis, Polyacrylamide Gel
Histone-Lysine N-Methyltransferase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Histones

Lysine

Methylation

Models, Genetic

Mutation

Nuclear Proteins

Phenotype

Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 11752412
DOI: 10.1073/pnas.221596698
PMCID: PMC117519

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-11752412-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3.PMID 11752412Read ↗

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