Structure-guided design of a methyl donor cofactor that controls a viral histone H3 lysine 27 methyltransferase activity

Jiaojie Li; Hua Wei; Ming Ming Zhou

doi:10.1021/jm201000j

Structure-guided design of a methyl donor cofactor that controls a viral histone H3 lysine 27 methyltransferase activity

Jiaojie Li, Hua Wei, Ming Ming Zhou

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

vSET (a viral SET domain protein) is an attractive polycomb repressive complex 2 (PRC2) surrogate to study the effect of histone H3 lysine 27 (H3K27) methylation on gene transcription, as both catalyze histone H3K27 trimethylation. To control the enzymatic activity of vSET in vivo with an engineered S-adenosyl-l-methionine (SAM) analogue as methyl donor cofactor, we have carried out structure-guided design, synthesis, and characterization of orthogonal vSET methyltransferase mutant/SAM analogue pairs using a "bump-and-hole" strategy.

Original language	English
Pages (from-to)	7734-7738
Number of pages	5
Journal	Journal of Medicinal Chemistry
Volume	54
Issue number	21
DOIs	https://doi.org/10.1021/jm201000j
State	Published - 10 Nov 2011

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abstract = "vSET (a viral SET domain protein) is an attractive polycomb repressive complex 2 (PRC2) surrogate to study the effect of histone H3 lysine 27 (H3K27) methylation on gene transcription, as both catalyze histone H3K27 trimethylation. To control the enzymatic activity of vSET in vivo with an engineered S-adenosyl-l-methionine (SAM) analogue as methyl donor cofactor, we have carried out structure-guided design, synthesis, and characterization of orthogonal vSET methyltransferase mutant/SAM analogue pairs using a {"}bump-and-hole{"} strategy.",

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AU - Wei, Hua

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AB - vSET (a viral SET domain protein) is an attractive polycomb repressive complex 2 (PRC2) surrogate to study the effect of histone H3 lysine 27 (H3K27) methylation on gene transcription, as both catalyze histone H3K27 trimethylation. To control the enzymatic activity of vSET in vivo with an engineered S-adenosyl-l-methionine (SAM) analogue as methyl donor cofactor, we have carried out structure-guided design, synthesis, and characterization of orthogonal vSET methyltransferase mutant/SAM analogue pairs using a "bump-and-hole" strategy.

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Structure-guided design of a methyl donor cofactor that controls a viral histone H3 lysine 27 methyltransferase activity

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