Non-canonical Staphylococcus aureus pathogenicity island repression
| Autor: | Laura Miguel-Romero, Mohammed Alqasmi, Julio Bacarizo, Jason A Tan, Richard J Cogdell, John Chen, Olwyn Byron, Gail E Christie, Alberto Marina, José R Penadés |
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| Přispěvatelé: | Biotechnology and Biological Sciences Research Council (BBSRC), Medical Research Council (MRC), Biotechnology and Biological Sciences Research Cou, Medical Research Council (UK), Biotechnology and Biological Sciences Research Council (UK), European Research Council, Ministerio de Economía y Competitividad (España), Ministerio de Ciencia e Innovación (España), Generalitat Valenciana, Ministerio de Educación (España), National Institutes of Health (US), Fundación Ramón Areces, Wolfson Foundation, Royal Society (UK), Marina, Alberto, Marina, Alberto [0000-0002-1334-5273], UCH. Departamento de Ciencias Biomédicas, Producción Científica UCH 2022 |
| Rok vydání: | 2022 |
| Předmět: |
Estafilococos
Biochemistry & Molecular Biology Staphylococcus aureus Genomic Islands 05 Environmental Sciences PROTEIN Genética molecular Genomics Genetics PARTICLES TOOL Molecular genetics Science & Technology Genómica Ácidos nucleicos DNA 06 Biological Sciences GENE FAMILY Staphylococcus 08 Information and Computing Sciences Molecular biology Nucleic acid Biología molecular Staphylococcus Phages Life Sciences & Biomedicine Developmental Biology |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
| ISSN: | 1362-4962 0305-1048 |
| Popis: | 19 páginas, 9 figuras, 1 tabla. Mobile genetic elements control their life cycles by the expression of a master repressor, whose function must be disabled to allow the spread of these elements in nature. Here, we describe an unprecedented repression-derepression mechanism involved in the transfer of Staphylococcus aureus pathogenicity islands (SaPIs). Contrary to the classical phage and SaPI repressors, which are dimers, the SaPI1 repressor StlSaPI1 presents a unique tetrameric conformation never seen before. Importantly, not just one but two tetramers are required for SaPI1 repression, which increases the novelty of the system. To derepress SaPI1, the phage-encoded protein Sri binds to and induces a conformational change in the DNA binding domains of StlSaPI1, preventing the binding of the repressor to its cognate StlSaPI1 sites. Finally, our findings demonstrate that this system is not exclusive to SaPI1 but widespread in nature. Overall, our results characterize a novel repression-induction system involved in the transfer of MGE-encoded virulence factors in nature. This work was supported by grants MR/V000772/1, MR/M003876/1 and MR/S00940X/1 from the Medical Research Council (UK), BB/N002873/1, BB/S003835/1 and BB/V002376/1 from the Biotechnology and Biological Sciences Research Council (BBSRC, UK), Wellcome Trust201531/Z/16/Z, and ERC-ADG-2014 Proposal n◦670932 Dut-signal from EU to J.R.P.; grants PID2019-108541GB-I00 from Spanish Government (Ministerio de Econom´ıa y Competitividad y Ministerio de Ciencia e Innovacion) and PROMETEO ´ /2020/012 from Valencian Government to A.M.; grants MOE2017-T2-2-163 and MOE2019-T2-2-162 from the Ministry of Education to J.C.; and grant NIHR01 AI083255 to G.C. J.T. was supported by NIH IRACDA Grant K12GM093857 to Virginia Commonwealth University. We acknowledge Diamond Light Source for time on Beamline I03 for X-ray crystallography and B21 for SEC-SAXS under Proposal 16258. L.M.-R. was the recipient of a Spanish postdoctoral fellowship from Fundacion Ram ´ on Areces (2018–2020). J.R.P. is ´thankful to the Royal Society and the Wolfson Foundation for providing him support through a Royal Society Wolfson Fellowship. Funding for open access charge: University funds. |
| Databáze: | OpenAIRE |
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