ArticleJournal of bacteriology2010
Biologically active isoforms of CobB sirtuin deacetylase in Salmonella enterica and Erwinia amylovora.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 39 citations in OpenAlex.
- PolyP inhibits CobB deacetylase triggering a regulatory coupling to prevent DNA replication initiation.Nucleic acids research · 2026Article
- InPathogens (Basel, Switzerland) · 2025Article
- YkuR functions as a protein deacetylase inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule.Nature communications · 2024Article
- Review
- Bacteria employ lysine acetylation of transcriptional regulators to adapt gene expression to cellular metabolism.Nature communications · 2024Article
- An insight into the role of the N-terminal domain ofFrontiers in molecular biosciences · 2024Article
- Structure and Function of Kdac1, a Class II Deacetylase from the Multidrug-Resistant PathogenBiochemistry · 2023Article
- The Acyl-Proteome of Syntrophus aciditrophicus Reveals Metabolic Relationships in Benzoate Degradation.Molecular & cellular proteomics : MCP · 2022Article
- Sirtuin-Dependent Reversible Lysine Acetylation Controls the Activity of Acetyl Coenzyme A Synthetase in Campylobacter jejuni.Journal of bacteriology · 2021Article
- Protein Acetyltransferases Mediate Bacterial Adaptation to a Diverse Environment.Journal of bacteriology · 2021Review
- Bacterial Sirtuins Overview: An Open Niche to Explore.Frontiers in microbiology · 2021Review
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- 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
- Interplay between the bacterial protein deacetylase CobB and the second messenger c-di-GMP.The EMBO journal · 2019Article
- Post-translational Protein Acetylation: An Elegant Mechanism for Bacteria to Dynamically Regulate Metabolic Functions.Frontiers in microbiology · 2019Review
- Article
- In Streptomyces lividans, acetyl-CoA synthetase activity is controlled by O-serine and NMolecular microbiology · 2018Article
- A Toxin Involved inmBio · 2017Article
- A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNA.Molecular cell · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Sirtuins are NAD(+)-dependent protein deacylases that are conserved in all domains of life and are involved in diverse cellular processes, including control of gene expression and central metabolism. Eukaryotic sirtuins have N-terminal extensions that have been linked to protein multimerization and cellular localization. Here the first evidence of sirtuin isoforms in bacteria is reported. The enterobacterium Salmonella enterica synthesizes two isoforms of CobB sirtuin, a shorter 236-amino-acid isoform (here CobB(S)) and a longer 273-amino-acid isoform (here CobB(L)). The N-terminal 37-amino-acid extension of CobB(L) is amphipathic, containing 18 basic amino acids (12 of which are Arg) and 13 hydrophobic ones; both isoforms were active in vivo and in vitro. Northern blot and transcription start site analyses revealed that cobB is primarily expressed as two monocistronic cobB mRNAs from two transcription start sites, one of which was mapped within the neighboring ycfX gene and the other of which was located within cobB. Additionally, a low-abundance ycfX-cobB bicistronic mRNA was observed which could encode up to three proteins (YcfX, CobB(L), and CobB(S)). CobB(L) isoforms are common within the family Enterobacteriaceae, but species of the genus Erwinia (including the plant pathogen Erwinia amylovora) encode only the CobB(L) isoform. The CobB(L) isoform from E. amylovora restored growth of as S. enterica cobB mutant strain on low acetate.
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Registered trials
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