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Class-A penicillin binding proteins do not contribute to cell shape but repair cell-wall defects.
Vigouroux, Antoine; Cordier, Baptiste; Aristov, Andrey; Alvarez, Laura; Özbaykal, Gizem; Chaze, Thibault; Oldewurtel, Enno Rainer; Matondo, Mariette; Cava, Felipe; Bikard, David; van Teeffelen, Sven.
Afiliación
  • Vigouroux A; Microbial Morphogenesis and Growth Laboratory, Institut Pasteur, Paris, France.
  • Cordier B; Synthetic Biology Laboratory, Institut Pasteur, Paris, France.
  • Aristov A; Université Paris Descartes, Sorbonne-Paris-Cité, Paris, France.
  • Alvarez L; Microbial Morphogenesis and Growth Laboratory, Institut Pasteur, Paris, France.
  • Özbaykal G; Microbial Morphogenesis and Growth Laboratory, Institut Pasteur, Paris, France.
  • Chaze T; Laboratory for Molecular Infection Medicine Sweden (MIMS), Umeå Centre for Microbial Research (UCMR), Department of Molecular Biology, Umeå University, Umeå, Sweden.
  • Oldewurtel ER; Microbial Morphogenesis and Growth Laboratory, Institut Pasteur, Paris, France.
  • Matondo M; Université Paris Diderot, Sorbonne-Paris-Cité, Paris, France.
  • Cava F; Proteomics Platform, Institut Pasteur, Paris, France.
  • Bikard D; Microbial Morphogenesis and Growth Laboratory, Institut Pasteur, Paris, France.
  • van Teeffelen S; Proteomics Platform, Institut Pasteur, Paris, France.
Elife ; 92020 01 06.
Article en En | MEDLINE | ID: mdl-31904338
Cell shape and cell-envelope integrity of bacteria are determined by the peptidoglycan cell wall. In rod-shaped Escherichia coli, two conserved sets of machinery are essential for cell-wall insertion in the cylindrical part of the cell: the Rod complex and the class-A penicillin-binding proteins (aPBPs). While the Rod complex governs rod-like cell shape, aPBP function is less well understood. aPBPs were previously hypothesized to either work in concert with the Rod complex or to independently repair cell-wall defects. First, we demonstrate through modulation of enzyme levels that aPBPs do not contribute to rod-like cell shape but are required for mechanical stability, supporting their independent activity. By combining measurements of cell-wall stiffness, cell-wall insertion, and PBP1b motion at the single-molecule level, we then present evidence that PBP1b, the major aPBP, contributes to cell-wall integrity by repairing cell wall defects.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pared Celular / Proteínas de Escherichia coli / Proteínas de Unión a las Penicilinas / Escherichia coli Idioma: En Revista: Elife Año: 2020 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido
Texto completo
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XML
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Pared Celular / Proteínas de Escherichia coli / Proteínas de Unión a las Penicilinas / Escherichia coli Idioma: En Revista: Elife Año: 2020 Tipo del documento: Article País de afiliación: Francia Pais de publicación: Reino Unido