ArticleMolecular microbiology2013
Acetoacetyl-CoA synthetase activity is controlled by a protein acetyltransferase with unique domain organization in Streptomyces lividans.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 49 citations in OpenAlex.
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- Degradation Mechanism of AAA+ Proteases and Regulation ofBiomolecules · 2022Review
- A novel strategy of gene screen based on multi-omics in Streptomyces roseosporus.Applied microbiology and biotechnology · 2022Article
- Comparative Genomics of Marine Bacteria from a Historically Defined Plastic Biodegradation Consortium with the Capacity to Biodegrade Polyhydroxyalkanoates.Microorganisms · 2021Article
- Genome-Wide Analyses of Proteome and Acetylome inFrontiers in microbiology · 2021Article
- Bacterial Sirtuins Overview: An Open Niche to Explore.Frontiers in microbiology · 2021Review
- Modulation of Gene Expression in Actinobacteria by Translational Modification of Transcriptional Factors and Secondary Metabolite Biosynthetic Enzymes.Frontiers in microbiology · 2021Review
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Deacetylation enhances ParB-DNA interactions affecting chromosome segregation in Streptomyces coelicolor.Nucleic acids research · 2020Article
- Crotonylation of key metabolic enzymes regulates carbon catabolite repression in Streptomyces roseosporus.Communications biology · 2020Article
- New AMP-forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylation.Molecular microbiology · 2020Article
- Protein Acetylation in Bacteria.Annual review of microbiology · 2019Review
- Functional Insights Into Protein Acetylation in the Hyperthermophilic ArchaeonMolecular & cellular proteomics : MCP · 2019Article
- Staphylococcus aureus modulates the activity of acetyl-Coenzyme A synthetase (Acs) by sirtuin-dependent reversible lysine acetylation.Molecular microbiology · 2019Article
- Protein acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27.Extremophiles : life under extreme conditions · 2019Article
- Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions.Frontiers in microbiology · 2019Review
- Article
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Authors and funding
2 authors at 2 institutions in 1 country.
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Abstract
GCN5-type N-acetyltransferases (GNATs) are enzymes that catalyse the transfer of the acetyl group from acetyl-CoA to a primary amine. GNATs are conserved in all domains of life. Some members of this family of enzymes acetylate the side-chain of specific lysine residues in proteins of diverse function. In bacteria, GNAT-catalysed protein acetylation regulates carbon metabolism, RNA metabolism and transcriptional regulation. Metabolic regulation in Streptomyces species is of interest due to the role of these organisms in natural product synthesis. Here we identify SlPatA, a GNAT in Streptomyces lividans with unique domain organization, and a new acetylation target, namely acetoacetyl-CoA synthetase (SlAacS). The latter has homologues in all domains of life. In vitro and in vivo evidence show that SlAacS is a bona fide acetoacetyl-CoA synthetase. SlPatA acetylates SlAacS more efficiently than it does acetyl-CoA synthetase, an enzyme known to be under acetylation control. SlPatA acetylates SlAacS at the active-site residue Lys617 and acetylation inactivates SlAacS. Acetylated SlAacS was deacetylated by a sirtuin-type protein deacetylase. SlAacS acetylation/deacetylation may represent a conserved mechanism for regulation of acetoacetyl-CoA synthetase activity in all domains of life.
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Registered trials
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