Substrate Scope for Human Histone Lysine Acetyltransferase KAT8 |
| |
| Authors: | Giordano Proietti Yali Wang Chiara Punzo Jasmin Mecinovi&#x; |
| |
| Affiliation: | 1.Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark; (G.P.); (C.P.);2.Institute for Molecules and Materials, Radboud University, Heyendaalseweg 135, 6525 AJ Nijmegen, The Netherlands;3.Department of Blood Transfusion, Jilin University, 126 Xiantai Street, Changchun 130033, China |
| |
| Abstract: | Biomedically important histone lysine acetyltransferase KAT8 catalyses the acetyl coenzyme A-dependent acetylation of lysine on histone and other proteins. Here, we explore the ability of human KAT8 to catalyse the acetylation of histone H4 peptides possessing lysine and its analogues at position 16 (H4K16). Our synthetic and enzymatic studies on chemically and structurally diverse lysine mimics demonstrate that KAT8 also has a capacity to acetylate selected lysine analogues that possess subtle changes on the side chain and main chain. Overall, this work highlights that KAT8 has a broader substrate scope beyond natural lysine, and contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase (KAT) family. |
| |
| Keywords: | acetylation epigenetics histone lysine posttranslational modifications |
|
|
