ArticleNucleic acids research2006
Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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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.
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Who cites it
56 citing papers in PubMed, 142 citations in OpenAlex.
- Silver nanoparticles as next-generation antimicrobial agents: mechanisms, challenges, and innovations against multidrug-resistant bacteria.Frontiers in cellular and infection microbiology · 2025Review
- Metabolic response of Klebsiella oxytoca to ciprofloxacin exposure: a metabolomics approach.Metabolomics : Official journal of the Metabolomic Society · 2024Article
- Molecular and microbiological methods for the identification of nonreplicating Mycobacterium tuberculosis.PLoS pathogens · 2024Review
- Thermophilic PHP Protein Tyrosine Phosphatases (Cap8C and Wzb) from Mesophilic Bacteria.International journal of molecular sciences · 2024Article
- Liquid-Liquid Phase Separation and Protective Protein Aggregates in Bacteria.Molecules (Basel, Switzerland) · 2023Review
- Applications of Silver Nanoparticles in Dentistry.Cureus · 2023Review
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Factors involved in heterologous expression of proteins in E. coli host.Archives of microbiology · 2023Review
- Effective decolonization strategy for mupirocin-resistantMaterials today. Bio · 2023Article
- Replication stalling activates SSB for recruitment of DNA damage tolerance factors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure-Morphology-Antimicrobial and Antiviral Activity Relationship in Silver-Containing Nanocomposites Based on Polylactide.Molecules (Basel, Switzerland) · 2022Article
- Review
- Antibacterial Profile of a Microbicidal Agent Targeting Tyrosine Phosphatases and Redox Thiols, Novel Drug Targets.Antibiotics (Basel, Switzerland) · 2021Article
- An ATPase with a twist: A unique mechanism underlies the activity of the bacterial tyrosine kinase, Wzc.Science advances · 2021Article
- Tyrosine Phosphorylation as a Widespread Regulatory Mechanism in Prokaryotes.Journal of bacteriology · 2019Review
- Porphyromonas gingivalis Tyrosine Phosphatase Php1 Promotes Community Development and Pathogenicity.mBio · 2019Article
- Multiple links connect central carbon metabolism to DNA replication initiation and elongation in Bacillus subtilis.DNA research : an international journal for rapid publication of reports on genes and genomes · 2018Article
- Phosphorylation of FtsZ and FtsA by a DNA Damage-Responsive Ser/Thr Protein Kinase Affects Their Functional Interactions inmSphere · 2018Article
- Phosphorylation of theFrontiers in microbiology · 2018Article
- Phosphorylation of Deinococcus radiodurans RecA Regulates Its Activity and May Contribute to Radioresistance.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-stranded DNA-binding proteins (SSBs) are required for repair, recombination and replication in all organisms. Eukaryotic SSBs are regulated by phosphorylation on serine and threonine residues. To our knowledge, phosphorylation of SSBs in bacteria has not been reported. A systematic search for phosphotyrosine-containing proteins in Streptomyces griseus by immunoaffinity chromatography identified bacterial SSBs as a novel target of bacterial tyrosine kinases. Since genes encoding protein-tyrosine kinases (PTKs) have not been recognized in streptomycetes, and SSBs from Streptomyces coelicolor (ScSSB) and Bacillus subtilis (BsSSB) share 38.7% identity, we used a B.subtilis protein-tyrosine kinase YwqD to phosphorylate two cognate SSBs (BsSSB and YwpH) in vitro. We demonstrate that in vivo phosphorylation of B.subtilis SSB occurs on tyrosine residue 82, and this reaction is affected antagonistically by kinase YwqD and phosphatase YwqE. Phosphorylation of B.subtilis SSB increased binding almost 200-fold to single-stranded DNA in vitro. Tyrosine phosphorylation of B.subtilis, S.coelicolor and Escherichia coli SSBs occured while they were expressed in E.coli, indicating that tyrosine phosphorylation of SSBs is a conserved process of post-translational modification in taxonomically distant bacteria.
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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.