Class-A penicillin binding proteins do not contribute to cell shape but repair cell- wall defects
| Autor: | Mariette Matondo, Enno R. Oldewurtel, Sven van Teeffelen, Antoine Vigouroux, Baptiste Cordier, Gizem Özbaykal, Felipe Cava, Andrey Aristov, Laura Alvarez, Thibault Chaze, David Bikard |
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| Přispěvatelé: | Biologie de Synthèse - Synthetic biology, Institut Pasteur [Paris], Morphogénèse et Croissance microbiennes / Microbial Morphogenesis and Growth, Université Paris Descartes - Paris 5 (UPD5), Université Sorbonne Paris Cité (USPC), Department of Molecular Biology [Umeå], Umeå University, Université Paris Diderot - Paris 7 (UPD7), Spectrométrie de Masse pour la Biologie – Mass Spectrometry for Biology (UTechS MSBio), Institut Pasteur [Paris]-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), This work was supported by the European Research Council (ERC) under the Europe Union’s Horizon 2020 research and innovation program [Grant Agreement No. (679980)], the French Government’s Investissement d’Avenir program Laboratoire d’Excellence ‘Integrative Biology of Emerging Infectious Diseases’ (ANR-10-LABX-62-IBEID), the Mairie de Paris ‘Emergence(s)’ program, and the Volkswagen Foundation. Research in the Cava lab is supported by MIMS, the Knut and Alice Wallenberg Foundation (KAW), the Swedish Research Council and the Kempe Foundation., ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), European Project: 679980,H2020,ERC-2015-STG,RCSB(2016), European Project: 677823,H2020,ERC-2015-STG,CRISPAIR(2016), Centre National de la Recherche Scientifique (CNRS)-Centre de Ressources et de Recherche Technologique - Center for Technological Resources and Research (C2RT), Institut Pasteur [Paris]-Institut Pasteur [Paris], ANR-10-LABX-62-IBEID,IBEID,Laboratoire d'Excellence 'Integrative Biology of Emerging Infectious Diseases'(2010), Institut Pasteur [Paris] (IP), Institut Pasteur [Paris] (IP)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Penicillin binding proteins
cell envelope QH301-705.5 Science infectious disease Cell Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology) Molecular Biology Microbiology Biochemistry or Biopharmacy) medicine.disease_cause General Biochemistry Genetics and Molecular Biology Cell wall 03 medical and health sciences chemistry.chemical_compound Cell Wall cell biology medicine Escherichia coli Biology (General) Medicinsk bioteknologi (med inriktning mot cellbiologi (inklusive stamcellsbiologi) molekylärbiologi mikrobiologi biokemi eller biofarmaci) 030304 developmental biology chemistry.chemical_classification 0303 health sciences Microbiology and Infectious Disease General Immunology and Microbiology 030306 microbiology single-molecule tracking penicillin-binding proteins General Neuroscience Escherichia coli Proteins microbiology E. coli CRISPRi General Medicine Cell Biology [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology peptidoglycan cell wall medicine.anatomical_structure Enzyme chemistry Biophysics cell-wall repair Medicine Peptidoglycan sense organs Cell envelope Cell wall repair Research Article |
| Zdroj: | eLife eLife, eLife Sciences Publication, 2020, 9, pp.e51998. ⟨10.7554/eLife.51998⟩ eLife, 2020, 9, pp.e51998. ⟨10.7554/eLife.51998⟩ eLife, Vol 9 (2020) |
| ISSN: | 2050-084X |
| Popis: | International audience; 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. |
| Databáze: | OpenAIRE |
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