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Updated: May 29, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
Structure-guided design of a methyl donor cofactor that controls a viral histone H3 lysine 27 methyltransferase
Jiaojie Li1, Hua Wei, Ming-Ming Zhou
1Department of Structural and Chemical Biology, Mount Sinai School of Medicine, New York, NY 10029, USA.
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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