The Acyl-CoA Specificity of Human Lysine Acetyltransferase KAT2A
OPEN ACCESS
Author / Producer
Date
2022-09-06
Publication Type
Journal Article
ETH Bibliography
yes
Citations
Altmetric
OPEN ACCESS
Data
Rights / License
Abstract
Protein post-translational modification sserve to regulate a broad range of cellular functions including signal transduction, transcription, and metabolism. Protein lysine residue sundergo many post-translational acylations and are regulated by a range of enzymes, such as histone acetyl transferases (HATs)and histone deacetylases (HDACs).KAT2A,well characterized as a lysine acetyltransferase for both histone and nonhistone substrates, has been reported to tolerate addition alacyl-CoA substrates, such as succinyl-CoA, and shows nonacetyl transferase activity in specific biologicalcontexts.In thiswork, we investigatethe acyl-CoA substrate preference of KAT2A and attempt to determine whether and to what extent addition alacyl-CoA substrates may be utilized by KAT2A in a cellula rcontext. We show that while KAT2A can bind and utilize malonyl-CoA, its activity with succinyl-CoA or glutaryl-CoA is very weak, and acetylation is still the most efficient activity for KAT2A in vitro and in cells.
Permanent link
Publication status
published
External links
Editor
Book title
Journal / series
Volume
61 (17)
Pages / Article No.
1874 - 1882
Publisher
American Chemical Society