title: Dual role for the O-acetyltransferase OatA in peptidoglycan modification and control of cell septation in Lactobacillus plantarum.
abstract: Until now, peptidoglycan O-acetyl transferases (Oat) were only described for their peptidoglycan O-acetylating activity and for their implication in the control of peptidoglycan hydrolases. In this study, we show that a Lactobacillus plantarum mutant lacking OatA is unable to uncouple cell elongation and septation. Wild-type cells showed an elongation arrest during septation while oatA mutant cells continued to elongate at a constant rate without any observable pause during the cell division process. Remarkably, this defect does not result from a default in peptidoglycan O-acetylation, since it can be rescued by wild-type OatA as well as by a catalytic mutant or a truncated variant containing only the transmembrane domain of the protein. Consistent with a potential involvement in division, OatA preferentially localizes at mid-cell before membrane invagination and remains at this position until the end of septation. Overexpression of oatA or its inactive variants induces septation-specific aberrations, including asymmetrical and dual septum formation. Overproduction of the division inhibitors, MinC or MinD, leads to cell filamentation in the wild type while curved and branched cells are observed in the oatA mutant, suggesting that the Min system acts differently on the division process in the absence of OatA. Altogether, the results suggest that OatA plays a key role in the spatio-temporal control of septation, irrespective of its catalytic activity.
authors.affiliation: Institut National de la Recherche Agronomique, UMR Micalis, Jouy-en-Josas, France.
authors.forename: Elvis
authors.initials: E
authors.lastname: Bernard
authors.forename: Thomas
authors.initials: T
authors.lastname: Rolain
authors.forename: Blandine
authors.initials: B
authors.lastname: David
authors.forename: Guillaume
authors.initials: G
authors.lastname: André
authors.forename: Vincent
authors.initials: V
authors.lastname: Dupres
authors.forename: Yves F
authors.initials: YF
authors.lastname: Dufrêne
authors.forename: Bernard
authors.initials: B
authors.lastname: Hallet
authors.forename: Marie-Pierre
authors.initials: MP
authors.lastname: Chapot-Chartier
authors.forename: Pascal
authors.initials: P
authors.lastname: Hols
mesh_terms: D000123:Acetyltransferases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D002455:Cell Division / Q000235:genetics / Q000502:physiology*; D049108:Cell Enlargement; D017931:DNA Primers / Q000235:genetics; D048191:Lactiplantibacillus plantarum / Q000201:enzymology* / Q000235:genetics; D008164:Luminescent Proteins; D018625:Microscopy, Atomic Force; D010457:Peptidoglycan / Q000378:metabolism*; D056951:Photoelectron Spectroscopy; D059008:Time-Lapse Imaging
chemical_list: D001426:Bacterial Proteins; D017931:DNA Primers; D008164:Luminescent Proteins; C080466:MinC protein, Bacteria; D010457:Peptidoglycan; C054562:yellow fluorescent protein, Bacteria; D000123:Acetyltransferases