ArticleJournal of bacteriology2008
Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme a synthetase (AcsA) in Bacillus subtilis.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed, 47 citations in OpenAlex.
- A Promising Strain for Wheat Growth Promotion and Antifungal Activity Against Fungal Phytopathogens:Microorganisms · 2026Article
- AcuB senses cellular energy charge to coordinate acetyl-CoA synthesis in bacteria.Nature communications · 2026Article
- A protein adaptor mediating Ap4A-dependent control of protein acetylation.Nature communications · 2026Article
- Regulation of acetyl-CoA biosynthesis via an intertwined acetyl-CoA synthetase/acetyltransferase complex.Nature communications · 2025Article
- Distribution and diversity of classical deacylases in bacteria.Nature communications · 2024Article
- Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.Nature communications · 2024Article
- The Acetyltransferase RibT FromFrontiers in microbiology · 2022Article
- Protein Acetyltransferases Mediate Bacterial Adaptation to a Diverse Environment.Journal of bacteriology · 2021Review
- Effects of acuC on the growth development and spinosad biosynthesis of Saccharopolyspora spinosa.Microbial cell factories · 2021Article
- Nutrient L-Alanine-Induced Germination ofFrontiers in microbiology · 2021Article
- Genome-Wide Analyses of Proteome and Acetylome inFrontiers in microbiology · 2021Article
- Modulation of the bacterial CobB sirtuin deacylase activity by N-terminal acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Staphylococcus aureus modulates the activity of acetyl-Coenzyme A synthetase (Acs) by sirtuin-dependent reversible lysine acetylation.Molecular microbiology · 2019Article
- YfmK is an NProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions.Frontiers in microbiology · 2019Review
- In-depth analysis of Bacillus subtilis proteome identifies new ORFs and traces the evolutionary history of modified proteins.Scientific reports · 2018Article
- In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and NMolecular microbiology · 2018Article
- Protein lysine acetylation plays a regulatory role in Bacillus subtilis multicellularity.PloS one · 2018Article
- Global Profiling of Lysine Acetylation inFrontiers in microbiology · 2018Article
- Regulation, Function, and Detection of Protein Acetylation in Bacteria.Journal of bacteriology · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The acuABC genes of Bacillus subtilis comprise a putative posttranslational modification system. The AcuA protein is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, the AcuC protein is a class I histone deacetylase, and the role of the AcuB protein is not known. AcuA controls the activity of acetyl coenzyme A synthetase (AcsA; EC 6.2.1.1) in this bacterium by acetylating residue Lys549. Here we report the kinetic analysis of wild-type and variant AcuA proteins. We contrived a genetic scheme for the identification of AcuA residues critical for activity. Changes at residues H177 and G187 completely inactivated AcuA and led to its rapid turnover. Changes at residues R42 and T169 were less severe. In vitro assay conditions were optimized, and an effective means of inactivating the enzyme was found. The basic kinetic parameters of wild-type and variant AcuA proteins were obtained and compared to those of eukaryotic GNATs. Insights into how the isolated mutations may exert their deleterious effect were investigated by using the crystal structure of an AcuA homolog.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.