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Abstract
Histone lysine acetyltransferase (KAT)-catalyzed acetylation of lysine residues in histone tails plays a key role in regulating gene expression in eukaryotes. Here, we examined the role of lysine side chain length in the catalytic activity of human KATs by incorporating shorter and longer lysine analogs into synthetic histone H3 and H4 peptides. The enzymatic activity of MOF, PCAF and GCN5 acetyltransferases towards histone peptides bearing lysine analogs was evaluated using MALDI-TOF MS assays. Our results demonstrate that human KAT enzymes have an ability to catalyze an efficient acetylation of longer lysine analogs, whereas shorter lysine analogs are not substrates for KATs. Kinetics analyses showed that lysine is a superior KAT substrate to its analogs with altered chain length, implying that lysine has an optimal chain length for KAT-catalyzed acetylation reaction.
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Details
1 University of Southern Denmark, Department of Physics, Chemistry and Pharmacy, Odense, Denmark (GRID:grid.10825.3e) (ISNI:0000 0001 0728 0170); Radboud University, Institute for Molecules and Materials, Nijmegen, The Netherlands (GRID:grid.5590.9) (ISNI:0000000122931605)
2 Radboud University, Institute for Molecules and Materials, Nijmegen, The Netherlands (GRID:grid.5590.9) (ISNI:0000000122931605); Jilin University, Department of Blood Transfusion, China-Japan Union Hospital, Changchun, People’s Republic of China (GRID:grid.64924.3d) (ISNI:0000 0004 1760 5735)
3 University of Southern Denmark, Department of Physics, Chemistry and Pharmacy, Odense, Denmark (GRID:grid.10825.3e) (ISNI:0000 0001 0728 0170)