Convergent evolution involving dimeric and trimeric dUTPases in pathogenicity island mobilization

• DOI: 10.1371/journal.ppat.1006581
• Publication Date: 2017-09-11T13:38:29Z
• Authors: Jorge Donderis; Janine Bowring; Elisa Maiques; J. Rafael Ciges-T...; Christian Alite; Iltyar Mehmedov; María Angeles Tor...; José R. Penadés; Alberto Marina
• Keywords: Pyrophosphatases/metabolism; Estafilococos.; 0301 basic medicine; PROTEIN; Binding Sites/physiology; 1108 Medical Microbiology; Signal Transduction/drug effects; CATALYTIC MECHANISM; CRYSTAL-STRUCTURE; Bacteriophages; Biology (General); Pyrophosphatases; TYPE-2 DUTPASE; 0303 health sciences; Bacteriophages/drug effects; 600; Amino Acid Sequence/physiology; FAMILY; 3. Good health; Staphylococcus.; Medical microbiology.; 1107 Immunology; Life Sciences & Biomedicine; 0605 Microbiology; Research Article; Signal Transduction; 570; Staphylococcus aureus; Genomic Islands; QH301-705.5; Microbiología médica.; Deoxyuracil Nucleotides/metabolism; INHIBITION; Medical bacteriology.; Microbiology; Pathogenic bacteria.; 03 medical and health sciences; Virology; REVEALS; Amino Acid Sequence; Science & Technology; Binding Sites; Repressor Proteins/metabolism; Bacteriología médica.; Staphylococcus aureus/enzymology; RC581-607; Repressor Proteins; Bacterias patógenas.; Parasitology; Immunologic diseases. Allergy; Protein Multimerization; Deoxyuracil Nucleotides; SYSTEM

The dUTPase (Dut) enzymes, encoded by almost all free-living organisms and some viruses, prevent the misincorporation of uracil into DNA. We previously proposed that trimeric Duts are regulatory proteins involved in different cellular processes; including phage-mediated transfer Staphylococcus aureus pathogenicity island SaPIbov1. Recently, it has been shown structurally unrelated dimeric Dut phage ϕNM1 is similarly able to mobilize SaPIbov1, suggesting could also be proteins. How this accomplished remains unsolved. Here, using vivo, biochemical structural approaches, we provide insights signaling mechanism used induce SaPIbov1 cycle. As reported for Duts, contain an extremely variable region, here named domain VI, which capacity these enzymes. Remarkably, our results show modulated dUTP, as with Duts. Overall, demonstrate although both sequence structure, control SaPI analogous mechanisms, representing a fascinating example convergent evolution. This conserved mode action highlights biological significance molecules.