PBP2b plays a key role in both peripheral growth and septum positioning in Lactococcus lactis

Autor:	Daniel Pérez-Núñez, Pascal Hols, Xavier De Bolle, Gabrielle Laurie Haustenne, Bernard Hallet, Marie-Pierre Chapot-Chartier, Blandine David, Eric Guédon, Marie-Clémence Duchêne
Přispěvatelé:	Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), Institut des Sciences de la Vie, Université Catholique de Louvain = Catholic University of Louvain (UCL), MICrobiologie de l'ALImentation au Service de la Santé (MICALIS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Microorg anisms Biology Research Unit (URBM ), Université de Namur [Namur] (UNamur), Science et Technologie du Lait et de l'Oeuf (STLO), Institut National de la Recherche Agronomique (INRA)-AGROCAMPUS OUEST, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), Hols, Pascal, Hallet, Bernard, Institut des Sciences de la Vie (ISV), Université Catholique de Louvain (UCL), Université de Namur [Namur]
Jazyk:	angličtina
Rok vydání:	2018
Předmět:	0301 basic medicine cell division Cell division lcsh:Medicine division cellulaire peptidoglycan Pathology and Laboratory Medicine Cell Fusion chemistry.chemical_compound Fluorescence Microscopy Cell Wall Lactococcus Medicine and Health Sciences Electron Microscopy Cell Cycle and Cell Division lcsh:Science Microscopy Multidisciplinary Cell fusion biology Chemistry Microbiology and Parasitology transpeptidase Phase Contrast Microscopy Light Microscopy lactoccocus lactis Pneumococcus Cell cycle peptidase Microbiologie et Parasitologie Bacterial Pathogens Cell biology [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Cell Processes Medical Microbiology Alimentation et Nutrition Pathogens microbiologie cellulaire Research Article peptidoglycan synthase PBP2b Cell Physiology Imaging Techniques 030106 microbiology beta-Lactams Research and Analysis Methods Microbiology 03 medical and health sciences lactococcus lactis Fluorescence Imaging Penicillin-Binding Proteins Food and Nutrition FtsZ Microbial Pathogens Bacteria Cell growth Lactococcus lactis lcsh:R Organisms Biofilm élongation cellulaire Biology and Life Sciences Streptococcus Cell Biology élongation biology.organism_classification peptidoglycane biology.protein Transmission Electron Microscopy lcsh:Q Peptidoglycan cathepsins [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
Zdroj:	PLoS ONE, Vol 13, Iss 5, p e0198014 (2018) PLoS ONE PLoS ONE, Public Library of Science, 2018, 13 (5), pp.e0198014. ⟨10.1371/journal.pone.0198014⟩ Plos One 5 (13), e0198014. (2018) David, B, Duchêne, M-C, Haustenne, G L, Pérez-Núñez, D, Chapot-Chartier, M-P, De Bolle, X, Guédon, E, Hols, P & Hallet, B 2018, ' PBP2b plays a key role in both peripheral growth and septum positioning in Lactococcus lactis ', PLoS ONE, vol. 13, no. 5, e0198014, pp. e0198014 . https://doi.org/10.1371/journal.pone.0198014
ISSN:	1932-6203
Popis:	Lactococcus lactis is an ovoid bacterium that forms filaments during planktonic and biofilm lifestyles by uncoupling cell division from cell elongation. In this work, we investigate the role of the leading peptidoglycan synthase PBP2b that is dedicated to cell elongation in ovococci. We show that the localization of a fluorescent derivative of PBP2b remains associated to the septal region and superimposed with structural changes of FtsZ during both vegetative growth and filamentation indicating that PBP2b remains intimately associated to the division machinery during the whole cell cycle. In addition, we show that PBP2b-negative cells of L. lactis are not only defective in peripheral growth; they are also affected in septum positioning. This septation defect does not simply result from the absence of the protein in the cell growth machinery since it is also observed when PBP2b-deficient cells are complemented by a catalytically inactive variant of PBP2b. Finally, we show that round cells resulting from β-lactam treatment are not altered in septation, suggesting that shape elongation as such is not a major determinant for selection of the division site. Altogether, we propose that the specific PBP2b transpeptidase activity at the septum plays an important role for tagging future division sites during L. lactis cell cycle.
Databáze:	OpenAIRE
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