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Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control

Julkaisun tekijätSzabo JE, Nemeth V, Papp-Kadar V, Nyiri K, Leveles I, Bendes AA, Zagyva I, Rona G, Palinkas HL, Besztercei B, Ozohanics O, Vekey K, Liliom K, Toth J, Vertessy BG



JournalNucleic Acids Research

Tietokannassa oleva lehden nimiNUCLEIC ACIDS RESEARCH

Lehden akronyymiNUCLEIC ACIDS RES



Lopetussivun numero11920

Sivujen määrä9



Transfer of phage-related pathogenicity islands of Staphylococcus aureus (SaPI-s) was recently reported to be activated by helper phage dUTPases. This is a novel function for dUTPases otherwise involved in preservation of genomic integrity by sanitizing the dNTP pool. Here we investigated the molecular mechanism of the dUTPase-induced gene expression control using direct techniques. The expression of SaPI transfer initiating proteins is repressed by proteins called Stl. We found that Phi 11 helper phage dUTPase eliminates SaPIbov1 Stl binding to its cognate DNA by binding tightly to Stl protein. We also show that dUTPase enzymatic activity is strongly inhibited in the dUTPase: Stl complex and that the dUTPase: dUTP complex is inaccessible to the Stl repressor. Our results disprove the previously proposed G-protein-like mechanism of SaPI transfer activation. We propose that the transfer only occurs if dUTP is cleared from the nucleotide pool, a condition promoting genomic stability of the virulence elements.

Last updated on 2022-27-09 at 08:15