+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Dual role for the O-acetyltransferase OatA in peptidoglycan modification and control of cell septation in Lactobacillus plantarum



Dual role for the O-acetyltransferase OatA in peptidoglycan modification and control of cell septation in Lactobacillus plantarum



Plos one 7(10): E47893



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.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 052726706

Download citation: RISBibTeXText

PMID: 23110121


Related references

OatA, a peptidoglycan O-acetyltransferase involved in Listeria monocytogenes immune escape, is critical for virulence. Journal of Infectious Diseases 204(5): 731-740, 2011

In vitro characterization of the antivirulence target of Gram-positive pathogens, peptidoglycan O-acetyltransferase A (OatA). Plos Pathogens 13(10): E1006667, 2017

Knockout of the alanine racemase gene in Lactobacillus plantarum results in septation defects and cell wall perforation. Fems Microbiology Letters 233(1): 131-138, 2004

Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS. 2012

Identification of key peptidoglycan hydrolases for morphogenesis, autolysis, and peptidoglycan composition of Lactobacillus plantarum WCFS1. Microbial Cell Factories 11: 137, 2012

Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Molecular Microbiology 55(3): 778-787, 2005

Peptidoglycan Modification by the Catalytic Domain of Streptococcus pneumoniae OatA Follows a Ping-Pong Bi-Bi Mechanism of Action. Biochemistry 57(16): 2394-2401, 2018

Immunoadjuvant activities of peptidoglycan subunits from the cell walls of Staphyloccus aureus and Lactobacillus plantarum. Biken Journal 18(2): 93, 1975

Selectivity for D-lactate incorporation into the peptidoglycan precursors of Lactobacillus plantarum: role of Aad, a VanX-like D-alanyl-D-alanine dipeptidase. Journal of Bacteriology 189(11): 4332-4337, 2007

Postsynthetic Modification of Bacterial Peptidoglycan Using Bioorthogonal N-Acetylcysteamine Analogs and Peptidoglycan O-Acetyltransferase B. Journal of the American Chemical Society 139(39): 13596-13599, 2017

Conservation characteristics of corn ears and stover ensiled with the addition of Lactobacillus plantarum MTD-1, Lactobacillus plantarum 30114, or Lactobacillus buchneri 11A44. Journal of Dairy Science 95(4): 2070-2080, 2012

Knockout of the two ldh genes has a major impact on peptidoglycan precursor synthesis in Lactobacillus plantarum. Journal of Bacteriology 178(18): 5431-5437, 1996

Lactobacillus plantarum lipoteichoic acid down-regulated Shigella flexneri peptidoglycan-induced inflammation. Molecular Immunology 48(4): 382-391, 2011

Identification of the amidotransferase AsnB1 as being responsible for meso-diaminopimelic acid amidation in Lactobacillus plantarum peptidoglycan. Journal of Bacteriology 193(22): 6323-6330, 2011

A simple radioisotopic assay for choline acetyltransferase and its application in the Lactobacillus plantarum system. Biochemical Pharmacology 15(4): 465-473, 1966