Roles of pneumococcal DivIB in cell division
| Autor: | Laure Roux, Audrey Le Gouellec, André Zapun, Thierry Vernet, Daniela Fadda, Orietta Massidda |
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| Přispěvatelé: | Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Le Gouellec, Audrey |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Cell division
MESH: Sequence Homology Amino Acid [SDV]Life Sciences [q-bio] Mutant Cell Cycle Proteins Plasma protein binding Cefotaxime MESH: Amino Acid Sequence MESH: Penicillin G MESH: INDEL Mutation INDEL Mutation Protein biosynthesis Microscopy Phase-Contrast MESH: Models Genetic Peptide sequence MESH: Bacterial Proteins MESH: Microscopy Phase-Contrast Genetics 0303 health sciences Penicillin G MESH: Cefotaxime Phenotype Cell biology [SDV] Life Sciences [q-bio] Streptococcus pneumoniae MESH: Microscopy Electron Transmission MESH: Cell Division MESH: Membrane Proteins Cell Division MESH: Streptococcus pneumoniae Protein Binding MESH: Microscopy Electron Scanning Molecular Sequence Data Biology Microbiology beta-Lactam Resistance Microbial Cell Biology 03 medical and health sciences MESH: Cell Cycle Proteins Bacterial Proteins Microscopy Electron Transmission MESH: Protein Binding Amino Acid Sequence Cell Cycle Protein Molecular Biology 030304 developmental biology MESH: Molecular Sequence Data Models Genetic Sequence Homology Amino Acid 030306 microbiology Membrane Proteins MESH: beta-Lactam Resistance Membrane protein Microscopy Electron Scanning |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2008, pp.4501-11 Journal of Bacteriology, 2008, pp.4501-11 |
| ISSN: | 0021-9193 1098-5530 |
| Popis: | DivIB, also known as FtsQ in gram-negative organisms, is a division protein that is conserved in most eubacteria. DivIB is localized at the division site and forms a complex with two other division proteins, FtsL and DivIC/FtsB. The precise function of these three bitopic membrane proteins, which are central to the division process, remains unknown. We report here the characterization of a divIB deletion mutant of Streptococcus pneumoniae , which is a coccus that divides with parallel planes. Unlike its homologue FtsQ in Escherichia coli , pneumococcal DivIB is not required for growth in rich medium, but the Δ divIB mutant forms chains of diplococci and a small fraction of enlarged cells with defective septa. However, the deletion mutant does not grow in a chemically defined medium. In the absence of DivIB and protein synthesis, the partner FtsL is rapidly degraded, whereas other division proteins are not affected, pointing to a role of DivIB in stabilizing FtsL. This is further supported by the finding that an additional copy of ftsL restores growth of the Δ divIB mutant in defined medium. Functional mapping of the three distinct α, β, and γ domains of the extracellular region of DivIB revealed that a complete β domain is required to fully rescue the deletion mutant. DivIB with a truncated β domain reverts only the chaining phenotype, indicating that DivIB has distinct roles early and late in the division process. Most importantly, the deletion of divIB increases the susceptibility to β-lactams, more evidently in a resistant strain, suggesting a function in cell wall synthesis. |
| Databáze: | OpenAIRE |
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