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Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif.

ABSTRACT: Although central to regulating the access to genetic information, most lysine methyltransferases remain poorly characterised relative to other family of enzymes. Herein, I report new substrates for the lysine methyltransferase SETD6. Based on the SETD6-catalysed site on the histone variant H2AZ, I identified similar sequences in the canonical histones H2A, H3, and H4 that are modified by SETD6 in vitro, and putative non-histone substrates. I herein expend the repertoire of substrates for methylation by SETD6.

SUBMITTER: Binda O

PROVIDER: S-EPMC6961689 | biostudies-literature | 2020 Jan - Feb

REPOSITORIES: biostudies-literature

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Lysine methyltransferase SETD6 modifies histones on a glycine-lysine motif.

Binda Olivier O

Epigenetics 20190801 1-2

Although central to regulating the access to genetic information, most lysine methyltransferases remain poorly characterised relative to other family of enzymes. Herein, I report new substrates for the lysine methyltransferase SETD6. Based on the SETD6-catalysed site on the histone variant H2AZ, I identified similar sequences in the canonical histones H2A, H3, and H4 that are modified by SETD6 <i>in vitro</i>, and putative non-histone substrates. I herein expend the repertoire of substrates for ...[more]

PMID: 31370726

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