ArticleMolecular & cellular proteomics : MCP2014
Lysine propionylation is a prevalent post-translational modification in Thermus thermophilus.
Article in Molecular & cellular proteomics : MCP, 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.
- Histone modification cross-talk: analytical tools and molecular mechanisms.The Biochemical journal · 2026Review
- Lysine Propionylation as a Metabolically Coupled PTM: Mechanisms, Functional Consequences, and Therapeutic Potentials.International journal of molecular sciences · 2026Review
- Propionylation of Fis K32 inFuture microbiology · 2025Article
- Recent Contributions of Proteomics to Our Understanding of Reversible NJournal of proteome research · 2024Review
- Substrate and Functional Diversity of Protein Lysine Post-translational Modifications.Genomics, proteomics & bioinformatics · 2024Review
- Review
- Regulation of the pyrimidine biosynthetic pathway by lysine acetylation of E. coli OPRTase.The FEBS journal · 2023Article
- Chromatin Structure and Dynamics: Focus on Neuronal Differentiation and Pathological Implication.Genes · 2022Review
- Propionylation of lysine, a new mechanism of short-chain fatty acids affecting bacterial virulence.American journal of translational research · 2022Review
- Detection of single peptide with only one amino acid modification via electronic fingerprinting using reengineered durable channel of Phi29 DNA packaging motor.Biomaterials · 2021Article
- A Transfer Learning-Based Approach for Lysine Propionylation Prediction.Frontiers in physiology · 2021Article
- Addressing the Possibility of a Histone-Like Code in Bacteria.Journal of proteome research · 2021Review
- Function and Mechanism of Novel Histone Posttranslational Modifications in Health and Disease.BioMed research international · 2021Review
- Lysine Propionylation is a Widespread Post-Translational Modification Involved in Regulation of Photosynthesis and Metabolism in Cyanobacteria.International journal of molecular sciences · 2019Article
- Protein acetylation on 2-isopropylmalate synthase from Thermus thermophilus HB27.Extremophiles : life under extreme conditions · 2019Article
- Integrated Succinylome and Metabolome Profiling Reveals Crucial Role of S-Ribosylhomocysteine Lyase in Quorum Sensing and Metabolism ofMolecular & cellular proteomics : MCP · 2019Article
- Proteome-Wide Identification of Lysine Propionylation in the Conidial and Mycelial Stages ofFrontiers in microbiology · 2019Article
- GlnR-Mediated Regulation of Short-Chain Fatty Acid Assimilation inFrontiers in microbiology · 2018Article
- 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
- Altered acetylation and succinylation profiles in Corynebacterium glutamicum in response to conditions inducing glutamate overproduction.MicrobiologyOpen · 2016Article
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4 authors.
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Abstract
Recent studies of protein post-translational modifications revealed that various types of lysine acylation occur in eukaryotic and bacterial proteins. Lysine propionylation, a newly discovered type of acylation, occurs in several proteins, including some histones. In this study, we identified 361 propionylation sites in 183 mid-exponential phase and late stationary phase proteins from Thermus thermophilus HB8, an extremely thermophilic eubacterium. Functional classification of the propionylproteins revealed that the number of propionylation sites in metabolic enzymes increased in late stationary phase, irrespective of protein abundance. The propionylation sites on proteins expressed in mid-exponential and late stationary phases partially overlapped. Furthermore, amino acid frequencies in the vicinity of propionylation sites differed, not only between the two growth phases but also relative to acetylation sites. In addition, 33.8% of mid-exponential phase-specific and 80.0% of late stationary phase-specific propionylations (n ≥ 2) implied that specific mechanisms regulate propionylation in the cell. Moreover, the limited degree of overlap between lysine propionylation (36.8%) and acetylation (49.2%) sites in 67 proteins that were both acetylated and propionylated strongly suggested that the two acylation reactions are regulated separately by specific enzymes and may serve different functions. Finally, we also found that eight propionylation sites overlapped with acetylation sites critical for protein functions such as Schiff-base formation and ligand binding.
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