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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Proietti G,Wang Y,Rainone G,Mecinović Jdoi
10.1038/s41598-020-69510-0subject
Has Abstractpub_date
2020-08-03 00:00:00pages
13046issue
1issn
2045-2322pii
10.1038/s41598-020-69510-0journal_volume
10pub_type
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