{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kieser KJ"],"funding":["HHS | National Institutes of Health","Howard Hughes Medical Institute","NIAID NIH HHS","NIGMS NIH HHS","PHS HHS","National Science Foundation"],"pagination":["13087-92"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4620856"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["112(42)"],"pubmed_abstract":["Peptidoglycan (PG), a complex polymer composed of saccharide chains cross-linked by short peptides, is a critical component of the bacterial cell wall. PG synthesis has been extensively studied in model organisms but remains poorly understood in mycobacteria, a genus that includes the important human pathogen Mycobacterium tuberculosis (Mtb). The principle PG synthetic enzymes have similar and, at times, overlapping functions. To determine how these are functionally organized, we carried out whole-genome transposon mutagenesis screens in Mtb strains deleted for ponA1, ponA2, and ldtB, major PG synthetic enzymes. We identified distinct factors required to sustain bacterial growth in the absence of each of these enzymes. We find that even the homologs PonA1 and PonA2 have unique sets of gene"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Peptidoglycan synthesis in Mycobacterium tuberculosis is organized into networks with varying drug susceptibility."],"pmcid":["PMC4620856"],"funding_grant_id":["n/a","F32 GM108355","DGE1144152 and DGE0946799","F32 A1093049","F32 GM108355-02","U01 GM094568","U19 AI107774"],"pubmed_authors":["Chao MC","Waldor MK","Sassetti CM","Kieser KJ","Ioerger TR","Sacchettini JC","Baranowski C","Long JE","Rubin EJ"],"additional_accession":[]},"is_claimable":false,"name":"Peptidoglycan synthesis in Mycobacterium tuberculosis is organized into networks with varying drug susceptibility.","description":"Peptidoglycan (PG), a complex polymer composed of saccharide chains cross-linked by short peptides, is a critical component of the bacterial cell wall. PG synthesis has been extensively studied in model organisms but remains poorly understood in mycobacteria, a genus that includes the important human pathogen Mycobacterium tuberculosis (Mtb). The principle PG synthetic enzymes have similar and, at times, overlapping functions. To determine how these are functionally organized, we carried out whole-genome transposon mutagenesis screens in Mtb strains deleted for ponA1, ponA2, and ldtB, major PG synthetic enzymes. We identified distinct factors required to sustain bacterial growth in the absence of each of these enzymes. We find that even the homologs PonA1 and PonA2 have unique sets of gene","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Oct","modification":"2026-05-09T15:48:19.925Z","creation":"2019-03-27T02:00:47Z"},"accession":"S-EPMC4620856","cross_references":{"pubmed":["26438867"],"doi":["10.1073/pnas.1514135112"]}}