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Structural Insight into Recognition of Methylated Histone H3K4 by Set3.

ABSTRACT: The plant homeodomain (PHD) finger of Set3 binds methylated lysine 4 of histone H3 in vitro and in vivo; however, precise selectivity of this domain has not been fully characterized. Here, we explore the determinants of methyllysine recognition by the PHD fingers of Set3 and its orthologs. We use X-ray crystallographic and spectroscopic approaches to show that the Set3 PHD finger binds di- and trimethylated states of H3K4 with comparable affinities and employs similar molecular mechanisms to form complexes with either mark. Composition of the methyllysine-binding pocket plays an essential role in determining the selectivity of the PHD fingers. The finding that the histone-binding activity is not conserved in the PHD finger of Set4 suggests different functions for the Set3 and Set4 paralogs.

SUBMITTER: Gatchalian J

PROVIDER: S-EPMC5374059 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature

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Structural Insight into Recognition of Methylated Histone H3K4 by Set3.

Gatchalian Jovylyn J Ali Muzaffar M Andrews Forest H FH Zhang Yi Y Barrett Alexander S AS Kutateladze Tatiana G TG

Journal of molecular biology 20160930 13

The plant homeodomain (PHD) finger of Set3 binds methylated lysine 4 of histone H3 in vitro and in vivo; however, precise selectivity of this domain has not been fully characterized. Here, we explore the determinants of methyllysine recognition by the PHD fingers of Set3 and its orthologs. We use X-ray crystallographic and spectroscopic approaches to show that the Set3 PHD finger binds di- and trimethylated states of H3K4 with comparable affinities and employs similar molecular mechanisms to for ...[more]

PMID: 27697561

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