Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.

doi:10.1038/35065132

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Article

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.

Nature - 1 Mar 2001

Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T

Abstract excerpt

Distinct modifications of histone amino termini, such as acetylation, phosphorylation and methylation, have been proposed to underlie a chromatin-based regulatory mechanism that modulates the accessibility of genetic information. In addition to histone modifications that facilitate gene activity, it is of similar importance to restrict inappropriate gene expression if cellular and developmental programmes are to...

Topics

Amino Acid Sequence
Animals
Binding Sites
Chromatin
DNA-Binding Proteins
Fibroblasts
Gene Expression Regulation
Hepatocyte Nuclear Factor 1
Hepatocyte Nuclear Factor 1-alpha
Hepatocyte Nuclear Factor 1-beta
Histone Methyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Histone-Lysine N-Methyltransferase

Histones

Humans

Lysine

Methylation

Methyltransferases

Mice

Source

Open in PubMed

Identifiers

PMID: 11242053
DOI: 10.1038/35065132

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-11242053-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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