ArticleJournal of bacteriology2014
The acetylation motif in AMP-forming Acyl coenzyme A synthetases contains residues critical for acetylation and recognition by the protein acetyltransferase pat of Rhodopseudomonas palustris.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 25 citations in OpenAlex.
- InJournal of bacteriology · 2026Article
- Machine learning reveals proteome-encoded growth determinants underlying metabolic versatility ofmSystems · 2026Article
- InbioRxiv : the preprint server for biology · 2026Article
- Machine Learning Reveals Proteome-Encoded Growth Predictors ofbioRxiv : the preprint server for biology · 2025Article
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- In Staphylococcus aureus, the acyl-CoA synthetase MbcS supports branched-chain fatty acid synthesis from carboxylic acid and aldehyde precursors.Molecular microbiology · 2024Article
- Acetylation of Lactate Dehydrogenase Negatively Regulates the Acidogenicity of Streptococcus mutans.mBio · 2022Article
- Substrate Specificity of the 3-Methylmercaptopropionyl Coenzyme A Dehydrogenase (DmdC1) from Ruegeria pomeroyi DSS-3.Applied and environmental microbiology · 2022Article
- Bacterial Sirtuins Overview: An Open Niche to Explore.Frontiers in microbiology · 2021Review
- New AMP-forming acid:CoA ligases from Streptomyces lividans, some of which are posttranslationally regulated by reversible lysine acetylation.Molecular microbiology · 2020Article
- Acetylome analysis of lysine acetylation in the plant pathogenic bacterium Brenneria nigrifluens.MicrobiologyOpen · 2020Article
- Staphylococcus aureus modulates the activity of acetyl-Coenzyme A synthetase (Acs) by sirtuin-dependent reversible lysine acetylation.Molecular microbiology · 2019Article
- Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions.Frontiers in microbiology · 2019Review
- In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and NMolecular microbiology · 2018Article
- Biochemical Characterization of the Lysine Acetylation of Tyrosyl-tRNA Synthetase in Escherichia coli.Chembiochem : a European journal of chemical biology · 2017Article
- Studying the Lysine Acetylation of Malate Dehydrogenase.Journal of molecular biology · 2017Article
- Proteome-wide identification of lysine propionylation in thermophilic and mesophilic bacteria: Geobacillus kaustophilus, Thermus thermophilus, Escherichia coli, Bacillus subtilis, and Rhodothermus marinus.Extremophiles : life under extreme conditions · 2017Article
- Temporal Regulation of themSystems · 2016Article
- Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.Microbiology and molecular biology reviews : MMBR · 2015Review
- Insights into the specificity of lysine acetyltransferases.The Journal of biological chemistry · 2014Article
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2 authors at 2 institutions in 1 country.
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Abstract
The AMP-forming acyl coenzyme A (acyl-CoA) synthetases are a large class of enzymes found in both anabolic and catabolic pathways that activate fatty acids to acyl-CoA molecules. The protein acetyltransferase (Pat) from Rhodopseudomonas palustris (RpPat) inactivates AMP-forming acyl-CoA synthetases by acetylating the ε-amino group of a conserved, catalytic lysine residue. In all of the previously described RpPat substrates, this lysine residue is located within a PX4GK motif that has been proposed to be a recognition motif for RpPat. Here, we report five new substrates for RpPat, all of which are also AMP-forming acyl-CoA synthetases. This finding supports the idea that Pat enzymes may have evolved to control the activity of this family of enzymes. Notably, RpPat did not acetylate the wild-type long-chain acyl-CoA synthetase B (RpLcsB; formerly Rpa2714) enzyme of this bacterium. However, a single amino acid change two residues upstream of the acetylation site was sufficient to convert RpLcsB into an RpPat substrate. The results of mutational and functional analyses of RpLcsB and RpPimA variants led us to propose PK/RTXS/T/V/NGKX2K/R as a substrate recognition motif. The underlined positions within this motif are particularly important for acetylation by RpPat. The first residue, threonine, is located 4 amino acids upstream of the acetylation site. The second residue can be S/T/V/N and is located two positions upstream of the acetylation site. Analysis of published crystal structures suggests that the side chains of these two residues are very close to the acetylated lysine residue, indicating that they may directly interact with RpPat.
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