期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 22, 期 2, 页码 -出版社
MDPI
DOI: 10.3390/ijms22020846
关键词
acetylation; epigenetics; histone; lysine; posttranslational modifications
资金
- European Research Council (ERC Starting Grant) [ChemEpigen-715691]
KAT8 is capable of acetylating selective lysine analogues with subtle changes in side chains and main chains, in addition to natural lysine. This study contributes to the design of new chemical probes targeting KAT8 and other members of the histone lysine acetyltransferase family.
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.
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