{"doi":"10.1101/2022.04.11.487844","title":"Peptidoglycan maturation controls spatiotemporal organisation of outer membrane proteins in\n                  <i>Escherichia coli</i>","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>\n                  Linkages between the outer membrane of Gram-negative bacteria and the peptidoglycan layer are crucial to the maintenance of cellular integrity and enable survival in challenging environments\n                  <jats:sup>1–5</jats:sup>\n                  . The functionality of the outer membrane relies on outer membrane proteins (OMPs), which are inserted by the β-barrel assembly machine, BAM\n                  <jats:sup>6, 7</jats:sup>\n                  . Previous work has shown that growing\n                  <jats:italic>Escherichia coli</jats:italic>\n                  cells segregate old OMPs towards the poles by an unknown mechanism\n                  <jats:sup>8</jats:sup>\n                  . Here, we demonstrate that peptidoglycan underpins the spatiotemporal organisation of OMPs. Mature, tetrapeptide-rich peptidoglycan binds to BAM components and suppresses OMP foldase activity. Nascent peptidoglycan, which is enriched in pentapeptides and concentrated at septa\n                  <jats:sup>9</jats:sup>\n                  , associates with BAM poorly and has little impact on its activity, leading to preferential insertion of OMPs at division sites. Synchronising OMP biogenesis to cell wall growth enables bacteria to replenish their OMPs by binary partitioning. Our study reveals that Gram-negative bacteria coordinate the assembly of two major cell envelope layers by rendering OMP biogenesis responsive to peptidoglycan maturation. This coordination offers new possibilities for the design of antibiotics that disrupt cell envelope integrity.\n                </jats:p>","journal":null,"year":null,"id":672856,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1011395,"name":"Federico Corona","orcid":"0000-0002-0743-5520","position":1,"is_corresponding":false},{"id":1758057,"name":"Ruth Cohen-Khait","orcid":null,"position":2,"is_corresponding":false},{"id":1453879,"name":"Dawei Sun","orcid":"0000-0003-1551-4349","position":3,"is_corresponding":false},{"id":1279025,"name":"Pooja Sridhar","orcid":"0000-0001-7933-7818","position":4,"is_corresponding":false},{"id":1279028,"name":"Timothy J. Knowles","orcid":"0000-0002-6632-0985","position":5,"is_corresponding":false},{"id":544238,"name":"Colin Kleanthous","orcid":"0000-0002-3273-0302","position":6,"is_corresponding":false},{"id":308355,"name":"Waldemar Vollmer","orcid":"0000-0003-0408-8567","position":7,"is_corresponding":false},{"id":1758056,"name":"Gideon Mamou","orcid":"0000-0003-0897-1680","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Peptidoglycan maturation controls spatiotemporal organisation of outer membrane proteins in\n                  <i>Escherichia coli</i>","abstract":"<jats:title>Abstract</jats:title>\n                <jats:p>\n                  Linkages between the outer membrane of Gram-negative bacteria and the peptidoglycan layer are crucial to the maintenance of cellular integrity and enable survival in challenging environments\n                  <jats:sup>1–5</jats:sup>\n                  . The functionality of the outer membrane relies on outer membrane proteins (OMPs), which are inserted by the β-barrel assembly machine, BAM\n                  <jats:sup>6, 7</jats:sup>\n                  . Previous work has shown that growing\n                  <jats:italic>Escherichia coli</jats:italic>\n                  cells segregate old OMPs towards the poles by an unknown mechanism\n                  <jats:sup>8</jats:sup>\n                  . Here, we demonstrate that peptidoglycan underpins the spatiotemporal organisation of OMPs. Mature, tetrapeptide-rich peptidoglycan binds to BAM components and suppresses OMP foldase activity. Nascent peptidoglycan, which is enriched in pentapeptides and concentrated at septa\n                  <jats:sup>9</jats:sup>\n                  , associates with BAM poorly and has little impact on its activity, leading to preferential insertion of OMPs at division sites. Synchronising OMP biogenesis to cell wall growth enables bacteria to replenish their OMPs by binary partitioning. Our study reveals that Gram-negative bacteria coordinate the assembly of two major cell envelope layers by rendering OMP biogenesis responsive to peptidoglycan maturation. This coordination offers new possibilities for the design of antibiotics that disrupt cell envelope integrity.\n                </jats:p>","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"19162232","pmcid":null,"openalex_id":"https://openalex.org/W4223589585","authors":[],"funders":[{"funder_name":"Biotechnology and Biological Sciences Research Council","grant_id":"BB/P009948/1","title":"Protein import through the E. coli cell envelope"},{"funder_name":"Wellcome Trust","grant_id":"201505/Z/16/Z","title":null},{"funder_name":"European Research Council","grant_id":"201505","title":"Protein Antibiotics: Discovery, mode of action and development"},{"funder_name":"European Research Council","grant_id":"742555","title":"Spatiotemporal organisation of bacterial outer membrane proteins"},{"funder_name":"Wellcome Trust","grant_id":"091911","title":"Advanced Microscopy for Chromosome and RNA Dynamics."},{"funder_name":"Wellcome Trust","grant_id":"107457","title":"Micron Oxford: super-resolution imaging of cellular dynamics."},{"funder_name":"European Commission","grant_id":"721484","title":"An integrated mulTidisciplinary appRoach towards a new generAtIon of aNtibiotics: Targeting function and cross-talk of bacterial Envelope proTein machineries"}],"total_grants":7,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"green","license":"cc-by-nc-nd","oa_locations":[{"url":"https://www.biorxiv.org/content/biorxiv/early/2022/04/25/2022.04.11.487844.full.pdf","host_type":"repository"},{"url":"https://www.biorxiv.org/content/biorxiv/early/2022/04/25/2022.04.11.487844.full.pdf","host_type":"repository"},{"url":"https://syndication.highwire.org/content/doi/10.1101/2022.04.11.487844","host_type":"publisher"},{"url":"https://doi.org/10.1101/2022.04.11.487844","host_type":"repository"},{"url":"https://europepmc.org/article/PPR/PPR480875","host_type":"Europe_PMC"},{"url":"https://europepmc.org/api/fulltextRepo?pprId=PPR480875&type=FILE&fileName=EMS144372-pdf.pdf&mimeType=application/pdf","host_type":"Europe_PMC"}],"fields_of_study":["Bacterial Genetics and Biotechnology","Escherichia coli research studies","Antibiotic Resistance in Bacteria","0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":[],"keywords":["Peptidoglycan","Bacterial outer membrane","Biogenesis","Cell envelope","Cell biology","Biology","Cell wall","Bacterial cell structure","Escherichia coli","Inner membrane","Bacteria","Microbiology","Biochemistry","Genetics"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"pdb"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T11:23:30.822366Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}