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Article

In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases.

The Journal of biological chemistry - 18 Feb 2005

Collins Robert E, Tachibana Makoto, Tamaru Hisashi, Smith Kristina M, Jia Da, Zhang Xing, Selker Eric U, Shinkai Yoichi, Cheng Xiaodong

Abstract excerpt

The functional significance of mono-, di-, and tri-methylation of lysine residues within histone proteins is under investigation. Evidence from several model organisms suggests that different methylated states of H3 Lys(9) (H3K9) are generated by specific histone methyltransferases (MTases) to mark distinct types of silent chromatin. Sequence alignment of all histone lysine MTases with known product specificity...

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Identifiers

PMID: 15590646
DOI: 10.1074/jbc.M410483200
PMCID: PMC2696276

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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