{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Aliashkevich A"],"funding":["Umeå Universitet","Vinnova","Vetenskapsrådet","Knut and Alice Wallenberg Stiftelse","Knut och Alice Wallenbergs Stiftelse","Swedish Research Council","Kempe Foundation","The Laboratory of Molecular Infection Medicine Sweden","University of Missouri","National Science Foundation"],"pagination":["e1011449"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11527210"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(10)"],"pubmed_abstract":["Peptidoglycan (PG), a mesh-like structure which is the primary component of the bacterial cell wall, is crucial to maintain cell integrity and shape. While most bacteria rely on penicillin binding proteins (PBPs) for crosslinking, some species also employ LD-transpeptidases (LDTs). Unlike PBPs, the essentiality and biological functions of LDTs remain largely unclear. The Hyphomicrobiales order of the Alphaproteobacteria, known for their polar growth, have PG which is unusually rich in LD-crosslinks, suggesting that LDTs may play a more significant role in PG synthesis in these bacteria. Here, we investigated LDTs in the plant pathogen Agrobacterium tumefaciens and found that LD-transpeptidation, resulting from at least one of 14 putative LDTs present in this bacterium, is essential for its"],"journal":["PLoS genetics"],"pubmed_title":["LD-transpeptidation is crucial for fitness and polar growth in Agrobacterium tumefaciens."],"pmcid":["PMC11527210"],"funding_grant_id":["URC-23-010","2023-02263","SMK2062","IOS1557806","KAW 2023.0346","2022-02958","JCK3126"],"pubmed_authors":["Aliashkevich A","Rea D","Gilmore MC","Typas A","Savitski MM","Alvarez L","Guest T","Mateus A","Cava F","Ruiz I","Brown PJB","Schiffthaler B","Amstutz J"],"additional_accession":[]},"is_claimable":false,"name":"LD-transpeptidation is crucial for fitness and polar growth in Agrobacterium tumefaciens.","description":"Peptidoglycan (PG), a mesh-like structure which is the primary component of the bacterial cell wall, is crucial to maintain cell integrity and shape. While most bacteria rely on penicillin binding proteins (PBPs) for crosslinking, some species also employ LD-transpeptidases (LDTs). Unlike PBPs, the essentiality and biological functions of LDTs remain largely unclear. The Hyphomicrobiales order of the Alphaproteobacteria, known for their polar growth, have PG which is unusually rich in LD-crosslinks, suggesting that LDTs may play a more significant role in PG synthesis in these bacteria. Here, we investigated LDTs in the plant pathogen Agrobacterium tumefaciens and found that LD-transpeptidation, resulting from at least one of 14 putative LDTs present in this bacterium, is essential for its","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-06-30T03:19:32.368Z","creation":"2025-04-21T21:51:19.845Z"},"accession":"S-EPMC11527210","cross_references":{"pubmed":["39432536"],"doi":["10.1371/journal.pgen.1011449"]}}