Highly potent dUTPase inhibition by a bacterial repressor protein reveals a novel mechanism for gene expression control
| Autor: | Veronika Papp-Kádár, Károly Liliom, Judit Tóth, Hajnalka L Pálinkás, Oliver Ozohanics, Imre Zagyva, Károly Vékey, Ábris Bendes, Judit Szabó, Veronika Németh, Gergely Róna, Kinga Nyíri, Balázs Besztercei, Ibolya Leveles, Beáta G. Vértessy |
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| Rok vydání: | 2014 |
| Předmět: |
Staphylococcus aureus
Genomic Islands Repressor Virulence Biology 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Gene expression Genetics Pyrophosphatases Transfer technique 030304 developmental biology chemistry.chemical_classification 0303 health sciences Gene regulation Chromatin and Epigenetics 030302 biochemistry & molecular biology Gene Expression Regulation Bacterial Pathogenicity island Molecular biology Cell biology Repressor Proteins Enzyme chemistry DNA Function (biology) |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gku882 |
| Popis: | 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 Φ11 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. |
| Databáze: | OpenAIRE |
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