ArticleThe Journal of biological chemistry2013
O-glycosylation as a novel control mechanism of peptidoglycan hydrolase activity.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Engineering galactoside acetyltransferase for enhanced hesperetin-7-O-glucoside bioavailability.Applied microbiology and biotechnology · 2026Article
- Commensal bacterial glycosylation at the interface of host-bacteria interactions.Gut microbes · 2025Review
- Review
- Antibacterial potential of a new glucosaminidase fromFrontiers in microbiology · 2025Article
- A comparative guide to expression systems for phage lysin production.Essays in biochemistry · 2024Review
- Article
- Effect of Protein O-Mannosyltransferase (MSMEG_5447) onFrontiers in microbiology · 2021Article
- Lysozyme Resistance in Clostridioides difficile Is Dependent on Two Peptidoglycan Deacetylases.Journal of bacteriology · 2020Article
- Study of theFrontiers in microbiology · 2020Article
- The Impact of Glycosylation of Osteopontin on Urinary Stone Formation.International journal of molecular sciences · 2019Article
- Distinct and Specific Role of NlpC/P60 Endopeptidases LytA and LytB in Cell Elongation and Division ofFrontiers in microbiology · 2019Article
- The Helicobacter pylori cell shape promoting protein Csd5 interacts with the cell wall, MurF, and the bacterial cytoskeleton.Molecular microbiology · 2018Article
- The increase of O-acetylation and N-deacetylation in cell wall promotes acid resistance and nisin production through improving cell wall integrity in Lactococcus lactis.Journal of industrial microbiology & biotechnology · 2018Article
- Streptomyces coelicolor strains lacking polyprenol phosphate mannose synthase and protein O-mannosyl transferase are hyper-susceptible to multiple antibiotics.Microbiology (Reading, England) · 2018Article
- How Sweet Are Our Gut Beneficial Bacteria? A Focus on Protein Glycosylation in Lactobacillus.International journal of molecular sciences · 2018Review
- SagB Glucosaminidase Is a Determinant of Staphylococcus aureus Glycan Chain Length, Antibiotic Susceptibility, and Protein Secretion.Journal of bacteriology · 2016Article
- The sweet tooth of bacteria: common themes in bacterial glycoconjugates.Microbiology and molecular biology reviews : MMBR · 2014Review
- O-Glycosylation of the N-terminal region of the serine-rich adhesin Srr1 of Streptococcus agalactiae explored by mass spectrometry.Molecular & cellular proteomics : MCP · 2014Article
- Cell wall structure and function in lactic acid bacteria.Microbial cell factories · 2014Review
- Biochemical characterization of the major N-acetylmuramidase from Lactobacillus buchneri.Microbiology (Reading, England) · 2014Article
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Authors and funding
12 authors at 5 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acm2, the major autolysin of Lactobacillus plantarum, is a tripartite protein. Its catalytic domain is surrounded by an O-glycosylated N-terminal region rich in Ala, Ser, and Thr (AST domain), which is of low complexity and unknown function, and a C-terminal region composed of five SH3b peptidoglycan (PG) binding domains. Here, we investigate the contribution of these two accessory domains and of O-glycosylation to Acm2 functionality. We demonstrate that Acm2 is an N-acetylglucosaminidase and identify the pattern of O-glycosylation (21 mono-N-acetylglucosamines) of its AST domain. The O-glycosylation process is species-specific as Acm2 purified from Lactococcus lactis is not glycosylated. We therefore explored the functional role of O-glycosylation by purifying different truncated versions of Acm2 that were either glycosylated or non-glycosylated. We show that SH3b domains are able to bind PG and are responsible for Acm2 targeting to the septum of dividing cells, whereas the AST domain and its O-glycosylation are not involved in this process. Notably, our data reveal that the lack of O-glycosylation of the AST domain significantly increases Acm2 enzymatic activity, whereas removal of SH3b PG binding domains dramatically reduces this activity. Based on this antagonistic role, we propose a model in which access of the Acm2 catalytic domain to its substrate may be hindered by the AST domain where O-glycosylation changes its conformation and/or mediates interdomain interactions. To the best of our knowledge, this is the first time that O-glycosylation is shown to control the activity of a bacterial enzyme.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.