Back to Search
Start Over
Modulation of plant acetyl-CoA synthetase activity by post-translational lysine acetylation
- Source :
- Frontiers in Molecular Biosciences, Vol 10 (2023)
- Publication Year :
- 2023
- Publisher :
- Frontiers Media S.A., 2023.
-
Abstract
- Acetyl-CoA synthetase (ACS) is one of several enzymes that generate the key metabolic intermediate, acetyl-CoA. In microbes and mammals ACS activity is regulated by the post-translational acetylation of a key lysine residue. ACS in plant cells is part of a two-enzyme system that maintains acetate homeostasis, but its post-translational regulation is unknown. This study demonstrates that the plant ACS activity can be regulated by the acetylation of a specific lysine residue that is positioned in a homologous position as the microbial and mammalian ACS sequences that regulates ACS activity, occurring in the middle of a conserved motif, near the carboxyl-end of the protein. The inhibitory effect of the acetylation of residue Lys-622 of the Arabidopsis ACS was demonstrated by site-directed mutagenesis of this residue, including its genetic substitution with the non-canonical N-ε-acetyl-lysine residue. This latter modification lowered the catalytic efficiency of the enzyme by a factor of more than 500-fold. Michaelis-Menten kinetic analysis of the mutant enzyme indicates that this acetylation affects the first half-reaction of the ACS catalyzed reaction, namely, the formation of the acetyl adenylate enzyme intermediate. The post-translational acetylation of the plant ACS could affect acetate flux in the plastids and overall acetate homeostasis.
Details
- Language :
- English
- ISSN :
- 2296889X
- Volume :
- 10
- Database :
- Directory of Open Access Journals
- Journal :
- Frontiers in Molecular Biosciences
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.23588e8a10744b6996137e138c5778fd
- Document Type :
- article
- Full Text :
- https://doi.org/10.3389/fmolb.2023.1117921