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Protein coopted from a phage restriction system dictates orthogonal cell division plane selection in Staphylococcus aureus.
Ramos-León, Félix; Anjuwon-Foster, Brandon R; Anantharaman, Vivek; Ferreira, Colby N; Ibrahim, Amany M; Tai, Chin-Hsien; Missiakas, Dominique M; Camberg, Jodi L; Aravind, L; Ramamurthi, Kumaran S.
Afiliação
  • Ramos-León F; Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, USA.
  • Anjuwon-Foster BR; Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, USA.
  • Anantharaman V; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, USA.
  • Ferreira CN; Department of Cell and Molecular Biology, University of Rhode Island, Kingston, USA.
  • Ibrahim AM; Department of Microbiology, Howard Taylor Ricketts Laboratory, University of Chicago, Lemont, USA.
  • Tai CH; Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, USA.
  • Missiakas DM; Department of Microbiology, Howard Taylor Ricketts Laboratory, University of Chicago, Lemont, USA.
  • Camberg JL; Department of Cell and Molecular Biology, University of Rhode Island, Kingston, USA.
  • Aravind L; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, USA.
  • Ramamurthi KS; Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, USA.
bioRxiv ; 2023 Sep 03.
Article em En | MEDLINE | ID: mdl-37886572
The spherical bacterium Staphylococcus aureus, a leading cause of nosocomial infections, undergoes binary fission by dividing in two alternating orthogonal planes, but the mechanism by which S. aureus correctly selects the next cell division plane is not known. To identify cell division placement factors, we performed a chemical genetic screen that revealed a gene which we termed pcdA. We show that PcdA is a member of the McrB family of AAA+ NTPases that has undergone structural changes and a concomitant functional shift from a restriction enzyme subunit to an early cell division protein. PcdA directly interacts with the tubulin-like central divisome component FtsZ and localizes to future cell division sites before membrane invagination initiates. This parallels the action of another McrB family protein, CTTNBP2, which stabilizes microtubules in animals. We show that PcdA also interacts with the structural protein DivIVA and propose that the DivIVA/PcdA complex recruits unpolymerized FtsZ to assemble along the proper cell division plane. Deletion of pcdA conferred abnormal, non-orthogonal division plane selection, increased sensitivity to cell wall-targeting antibiotics, and reduced virulence in a murine infection model. Targeting PcdA could therefore highlight a treatment strategy for combatting antibiotic-resistant strains of S. aureus.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: BioRxiv Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Idioma: En Revista: BioRxiv Ano de publicação: 2023 Tipo de documento: Article País de afiliação: Estados Unidos