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.

KEYWORDS:

• Chromatin
• histone
• lysine methyltransferase
• methylation
• SETD6

Acknowledgments

OB was supported by the Newcastle’s Biomedical Fellowship Programme, which is in part funded through the Wellcome Trust’s Institutional Strategic Support Fund, and by the Breast Cancer Campaign charity grant number 2013MaySP005.

Disclosure statement

No potential conflict of interest was reported by the author.

Supplementary material

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Correction Statement

This article has been republished with minor changes. These changes do not impact the academic content of the article.

Additional information

Funding

This work was supported by the Breast Cancer Campaign [2013MaySP005].