The structure of a polygamous repressor reveals how phage-inducible chromosomal islands spread in nature
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The structure of a polygamous repressor reveals how phage-inducible chromosomal islands spread in nature. / Ciges-Tomas, J Rafael; Alite, Christian; Humphrey, Suzanne; Donderis, J; Bowring, Janine; Salvatella, Xavier; Penadés, José R; Marina, Alberto.
I: Nature Communications, Bind 10, Nr. 1, 2019, s. 3676.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - The structure of a polygamous repressor reveals how phage-inducible chromosomal islands spread in nature
AU - Ciges-Tomas, J Rafael
AU - Alite, Christian
AU - Humphrey, Suzanne
AU - Donderis, J
AU - Bowring, Janine
AU - Salvatella, Xavier
AU - Penadés, José R
AU - Marina, Alberto
PY - 2019
Y1 - 2019
N2 - Stl is a master repressor encoded by Staphylococcus aureus pathogenicity islands (SaPIs) that maintains integration of these elements in the bacterial chromosome. After infection or induction of a resident helper phage, SaPIs are de-repressed by specific interactions of phage proteins with Stl. SaPIs have evolved a fascinating mechanism to ensure their promiscuous transfer by targeting structurally unrelated proteins performing identically conserved functions for the phage. Here we decipher the molecular mechanism of this elegant strategy by determining the structure of SaPIbov1 Stl alone and in complex with two structurally unrelated dUTPases from different S. aureus phages. Remarkably, SaPIbov1 Stl has evolved different domains implicated in DNA and partner recognition specificity. This work presents the solved structure of a SaPI repressor protein and the discovery of a modular repressor that acquires multispecificity through domain recruiting. Our results establish the mechanism that allows widespread dissemination of SaPIs in nature.
AB - Stl is a master repressor encoded by Staphylococcus aureus pathogenicity islands (SaPIs) that maintains integration of these elements in the bacterial chromosome. After infection or induction of a resident helper phage, SaPIs are de-repressed by specific interactions of phage proteins with Stl. SaPIs have evolved a fascinating mechanism to ensure their promiscuous transfer by targeting structurally unrelated proteins performing identically conserved functions for the phage. Here we decipher the molecular mechanism of this elegant strategy by determining the structure of SaPIbov1 Stl alone and in complex with two structurally unrelated dUTPases from different S. aureus phages. Remarkably, SaPIbov1 Stl has evolved different domains implicated in DNA and partner recognition specificity. This work presents the solved structure of a SaPI repressor protein and the discovery of a modular repressor that acquires multispecificity through domain recruiting. Our results establish the mechanism that allows widespread dissemination of SaPIs in nature.
KW - Biological Coevolution
KW - Crystallography, X-Ray
KW - DNA-Binding Proteins/genetics
KW - Genomic Islands/genetics
KW - Models, Molecular
KW - Staphylococcus Phages/genetics
KW - Staphylococcus aureus/genetics
U2 - 10.1038/s41467-019-11504-2
DO - 10.1038/s41467-019-11504-2
M3 - Journal article
C2 - 31417084
VL - 10
SP - 3676
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
ER -
ID: 373881907