• Medientyp: E-Artikel
  • Titel: Functional Characterization of COG1713 (YqeK) as a Novel Diadenosine Tetraphosphate Hydrolase Family
  • Beteiligte: Minazzato, Gabriele; Gasparrini, Massimiliano; Amici, Adolfo; Cianci, Michele; Mazzola, Francesca; Orsomando, Giuseppe; Sorci, Leonardo; Raffaelli, Nadia
  • Erschienen: American Society for Microbiology, 2020
  • Erschienen in: Journal of Bacteriology, 202 (2020) 10
  • Sprache: Englisch
  • DOI: 10.1128/jb.00053-20
  • ISSN: 1098-5530; 0021-9193
  • Schlagwörter: Molecular Biology ; Microbiology
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  • Beschreibung: <jats:p> Elevation of Ap <jats:sub>4</jats:sub> A level in bacteria is associated with increased sensitivity to heat and oxidative stress, reduced antibiotic tolerance, and decreased pathogenicity. ApaH is the major Ap <jats:sub>4</jats:sub> A hydrolase in gamma- and betaproteobacteria and has been recently proposed as a novel target to weaken the bacterial resistance to antibiotics. Here, we identified the orphan YqeK protein family (COG1713) as a highly efficient Ap <jats:sub>4</jats:sub> A hydrolase family, with members distributed in a consistent group of bacterial species that lack the ApaH enzyme. Among them are the pathogens <jats:named-content content-type="genus-species">Staphylococcus aureus</jats:named-content> , <jats:named-content content-type="genus-species">Streptococcus pneumoniae</jats:named-content> , and <jats:named-content content-type="genus-species">Mycoplasma pneumoniae</jats:named-content> . By identifying the player contributing to Ap <jats:sub>4</jats:sub> A homeostasis in these bacteria, we disclose a novel target to develop innovative antibacterial strategies. </jats:p>
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