5MIL

Pirating conserved phage mechanisms promotes promiscuous staphylococcal pathogenicity islands transfer.

Summary for 5MIL

• Entry DOI: 10.2210/pdb5mil/pdb
• Descriptor: DUTPase family protein, 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: dutpase, dimeric dutpase, deoxyuridine triphosphatase, hydrolase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 2
• Total formula weight: 46821.58

Authors

Donderis, J.,Marina, A.,Penades, J.R. (deposition date: 2016-11-28, release date: 2017-09-06, Last modification date: 2024-05-08)

Primary citation

Bowring, J.,Neamah, M.M.,Donderis, J.,Mir-Sanchis, I.,Alite, C.,Ciges-Tomas, J.R.,Maiques, E.,Medmedov, I.,Marina, A.,Penades, J.R.
Pirating conserved phage mechanisms promotes promiscuous staphylococcal pathogenicity island transfer.
Elife, 6:-, 2017

PubMed Abstract: Targeting conserved and essential processes is a successful strategy to combat enemies. Remarkably, the clinically important pathogenicity islands (SaPIs) use this tactic to spread in nature. SaPIs reside passively in the host chromosome, under the control of the SaPI-encoded master repressor, Stl. It has been assumed that SaPI de-repression is effected by specific phage proteins that bind to Stl, initiating the SaPI cycle. Different SaPIs encode different Stl repressors, so each targets a specific phage protein for its de-repression. Broadening this narrow vision, we report here that SaPIs ensure their promiscuous transfer by targeting conserved phage mechanisms. This is accomplished because the SaPI Stl repressors have acquired different domains to interact with unrelated proteins, encoded by different phages, but in all cases performing the same conserved function. This elegant strategy allows intra- and inter-generic SaPI transfer, highlighting these elements as one of nature's most fascinating subcellular parasites.

PubMed: 28826473
DOI: 10.7554/eLife.26487

Experimental method

X-RAY DIFFRACTION (2.1 Å)