The structure of a polygamous repressor reveals how phage-inducible chromosomal islands spread in nature

Autor: Suzanne Humphrey, Janine Bowring, José R. Penadés, Christian Alite, Xavier Salvatella, Jorge Donderis, Alberto Marina, J. Rafael Ciges-Tomas
Přispěvatelé: Ministerio de Economía y Competitividad (España), Generalitat Valenciana, Medical Research Council (UK), Biotechnology and Biological Sciences Research Council (UK), Wellcome Trust, Royal Society (UK), Wolfson Foundation, European Research Council, Marina, Alberto, Marina, Alberto [0000-0002-1334-5273]
Jazyk: angličtina
Rok vydání: 2019
Předmět:
0301 basic medicine
Models
Molecular
Staphylococcus Phages
DNA-BINDING DOMAINS
General Physics and Astronomy
02 engineering and technology
Crystallography
X-Ray
Biological Coevolution
chemistry.chemical_compound
CATALYTIC MECHANISM
lcsh:Science
Genetics
Multidisciplinary
INDUCTION
021001 nanoscience & nanotechnology
3. Good health
Multidisciplinary Sciences
DNA-Binding Proteins
Molecular mechanism
Science & Technology - Other Topics
0210 nano-technology
EXPRESSION
Staphylococcus aureus
Genomic Islands
PROTEINS
Science
Repressor
Phage biology
Biology
DNA-binding protein
Article
General Biochemistry
Genetics and Molecular Biology
03 medical and health sciences
X-ray crystallography
Science & Technology
Circular bacterial chromosome
General Chemistry
DNA-binding domain
Pathogenicity island
030104 developmental biology
chemistry
REPLICATION
lcsh:Q
DUTPASES
DNA
SYSTEM
Coevolution
Zdroj: Nature Communications
Nature Communications, Vol 10, Iss 1, Pp 1-16 (2019)
Digital.CSIC. Repositorio Institucional del CSIC
instname
ISSN: 2016-7857
2041-1723
Popis: 16 páginas, 7 figuras, 2 tablas. Coordinates and structure factors have been deposited in the Protein Data Bank under accession code 6H48, 6H4B, 6H49, 6H4C.
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.
This work was supported by grant BIO2016-78571-P from the Ministerio de Economia y Competitividad (Spain) and grant Prometeo II/2014/029 from Valencian Government (Spain) to A.M., and grants MR/M003876/1 and MR/S00940X/1 from the Medical Research Council (UK), BB/N002873/1 and BB/S003835/1 from the Biotechnology and Biological Sciences Research Council (BBSRC, UK), Wellcome Trust 201531/Z/16/Z, and ERC-ADG-2014 Proposal no. 670932 Dut-signal from EU to J.R.P. C.A. and J.R.C were supported by FPI BES-2014-068617 and FPU13/02880 predoctoral fellowships respectively. X-ray diffraction data collection was supported by Diamond Light Source block allocation group (BAG) Proposal MX14739 and MX16258 and Spanish Synchrotron Radiation Facility ALBA Proposal 2016071762 and 2017072262. J.R.P. is thankful to the Royal Society and the Wolfson Foundation for providing him support through a Royal Society Wolfson Fellowship.
Databáze: OpenAIRE
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