ArticleMolecular microbiology2015
Protein acetylation dynamics in response to carbon overflow in Escherichia coli.
Article in Molecular microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
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Who cites it
92 citing papers in PubMed, 159 citations in OpenAlex.
- The acetylation mechanism and engineering strategy of isocitrate lyase for optimizing biosynthesis inSynthetic and systems biotechnology · 2026Article
- The dual role of cAMP receptor protein (CRP) in regulating type 3 fimbriae expression in Klebsiella pneumoniae CG43S3 in response to oxygen availability.BMC microbiology · 2026Article
- Dynamic Lysine Acetylation Disrupts Isocitrate Lyase Function and Enables Metabolic Optimisation.Microbial biotechnology · 2026Article
- Bioorthogonal Click Chemistry for Antibody-Free Profiling of Acetylation, Propionylation, and Butyrylation inACS infectious diseases · 2026Article
- PolyP inhibits CobB deacetylase triggering a regulatory coupling to prevent DNA replication initiation.Nucleic acids research · 2026Article
- Reciprocal control of metabolic and chromatin regulators improves rice tolerance to heat.Nature communications · 2025Article
- AProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Modular pathway engineering for enhanced production ofApplied and environmental microbiology · 2025Article
- Intracellular acetyl phosphate modulatesActa biochimica et biophysica Sinica · 2025Article
- Functional consequences of lysine acetylation of phosphofructokinase isozymes.The FEBS journal · 2025Article
- Survival strategies of mycoplasmas: the critical role of post-translational modifications.Frontiers in cellular and infection microbiology · 2025Review
- Sensitivities in protein allocation models reveal distribution of metabolic capacity and flux control.Bioinformatics (Oxford, England) · 2024Article
- Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.Nature communications · 2024Article
- The activity of CobB1 protein deacetylase contributes to nucleoid compaction in Streptomyces venezuelae spores by increasing HupS affinity for DNA.Nucleic acids research · 2024Article
- Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator.PLoS genetics · 2024Article
- Relative impact of three growth conditions on theiScience · 2024Article
- Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024Review
- Characterizing lysine acetylation of glucokinase.Protein science : a publication of the Protein Society · 2024Article
- Global profiling of ribosomal protein acetylation reveals essentiality of acetylation homeostasis in maintaining ribosome assembly and function.Nucleic acids research · 2023Article
- Acetylation coordinates the crosstalk between carbon metabolism and ammonium assimilation in Salmonella enterica.The EMBO journal · 2023Article
32 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
In Escherichia coli, acetylation of proteins at lysines depends largely on a non-enzymatic acetyl phosphate-dependent mechanism. To assess the functional significance of this post-translational modification, we first grew wild-type cells in buffered tryptone broth with glucose and monitored acetylation over time by immunochemistry. Most acetylation occurred in stationary phase and paralleled glucose consumption and acetate excretion, which began upon entry into stationary phase. Transcription of rprA, a stationary phase regulator, exhibited similar behavior. To identify sites and substrates with significant acetylation changes, we used label-free, quantitative proteomics to monitor changes in protein acetylation. During growth, both the number of identified sites and the extent of acetylation increased with considerable variation among lysines from the same protein. As glucose-regulated lysine acetylation was predominant in central metabolic pathways and overlapped with acetyl phosphate-regulated acetylation sites, we deleted the major carbon regulator CRP and observed a dramatic loss of acetylation that could be restored by deleting the enzyme that degrades acetyl phosphate. We propose that acetyl phosphate-dependent acetylation is a response to carbon flux that could regulate central metabolism.
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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.