{"doi":"10.1128/mbio.03222-19","title":"Chlamydial MreB Directs Cell Division and Peptidoglycan Synthesis in Escherichia coli in the Absence of FtsZ Activity","abstract":"<jats:p>\n            The study of\n            <jats:italic>Chlamydia</jats:italic>\n            growth and cell division is complicated by its obligate intracellular nature and biphasic lifestyle.\n            <jats:italic>Chlamydia</jats:italic>\n            also lacks the universal division protein FtsZ. We employed the cell division system of\n            <jats:named-content content-type=\"genus-species\">Escherichia coli</jats:named-content>\n            as a surrogate to identify chlamydial cell division proteins. We demonstrate that chlamydial MreB, together with chlamydial RodZ, forms a cell division and growth complex that can replace FtsZ activity and support cell division in\n            <jats:named-content content-type=\"genus-species\">E. coli</jats:named-content>\n            . Chlamydial RodZ plays a major role in directing chlamydial MreB localization to the cell division site. It is likely that the evolution of chlamydial MreB and RodZ to form a functional cell division complex allowed\n            <jats:italic>Chlamydia</jats:italic>\n            to dispense with its FtsZ-based cell division machinery during genome reduction. Thus, MreB-RodZ represents a possible mechanism for cell division in other bacteria lacking FtsZ.\n          </jats:p>","journal":"mBio","year":2020,"id":614671,"datarank":0.4636563680037475,"base_score":3.091042453358316,"endowment":3.091042453358316,"self_citation_contribution":0.4636563680037475,"citation_network_contribution":0.0,"self_endowment_contribution":0.4636563680037475,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":21,"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":701981,"name":"George W. Liechti","orcid":"0000-0003-3028-8474","position":1,"is_corresponding":false},{"id":961538,"name":"Anthony T. Maurelli","orcid":"0000-0002-4788-6166","position":2,"is_corresponding":false},{"id":763977,"name":"Dev K. Ranjit","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Chlamydial MreB Directs Cell Division and Peptidoglycan Synthesis in Escherichia coli in the Absence of FtsZ Activity","abstract":"<jats:p>\n            The study of\n            <jats:italic>Chlamydia</jats:italic>\n            growth and cell division is complicated by its obligate intracellular nature and biphasic lifestyle.\n            <jats:italic>Chlamydia</jats:italic>\n            also lacks the universal division protein FtsZ. We employed the cell division system of\n            <jats:named-content content-type=\"genus-species\">Escherichia coli</jats:named-content>\n            as a surrogate to identify chlamydial cell division proteins. We demonstrate that chlamydial MreB, together with chlamydial RodZ, forms a cell division and growth complex that can replace FtsZ activity and support cell division in\n            <jats:named-content content-type=\"genus-species\">E. coli</jats:named-content>\n            . Chlamydial RodZ plays a major role in directing chlamydial MreB localization to the cell division site. It is likely that the evolution of chlamydial MreB and RodZ to form a functional cell division complex allowed\n            <jats:italic>Chlamydia</jats:italic>\n            to dispense with its FtsZ-based cell division machinery during genome reduction. Thus, MreB-RodZ represents a possible mechanism for cell division in other bacteria lacking FtsZ.\n          </jats:p>","is_dataset_classified":null,"base_score":3.091042453358316,"endowment":3.091042453358316,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"32071268","pmcid":"PMC7029139","openalex_id":"https://openalex.org/W3008215279","authors":[],"funders":[{"funder_name":"HHS | NIH | National Institute of Allergy and Infectious Diseases","grant_id":"R01AI123300","title":null},{"funder_name":"National Institutes of Health","grant_id":"5R01AI123300-04","title":"Peptidoglycan Assembly, Degradation, and Function in Pathogenic Chlamydia"}],"total_grants":2,"fwci":2.0876,"citation_percentile":0.86209588,"influential_citations":0,"citation_trend":[{"year":2019,"count":1},{"year":2020,"count":3},{"year":2021,"count":7},{"year":2022,"count":4},{"year":2023,"count":2},{"year":2024,"count":1},{"year":2025,"count":2},{"year":2026,"count":1}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://mbio.asm.org/content/mbio/11/1/e03222-19.full.pdf","host_type":"journal"},{"url":"https://mbio.asm.org/content/mbio/11/1/e03222-19.full.pdf","host_type":"publisher"},{"url":"https://journals.asm.org/doi/pdf/10.1128/mBio.03222-19","host_type":"publisher"},{"url":"https://doi.org/10.1128/mbio.03222-19","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/32071268","host_type":"repository"},{"url":"https://doaj.org/article/5b9d24f820e04c92a6f8c1225fa85350","host_type":"repository"},{"url":"https://doaj.org/article/8ab6b8e4b99d43a6bd19698dee9c1941","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/7029139","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC7029139","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC7029139?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1128/mBio.03222-19","host_type":""},{"url":"https://dx.doi.org/10.1128/mbio.03222-19","host_type":""}],"fields_of_study":["Reproductive tract infections research","Urinary Tract Infections Management","Escherichia coli research studies","0301 basic medicine","03 medical and health sciences"],"mesh_terms":["Bacterial Proteins","Cell Division","Cell Wall","Chlamydia","Cytoskeletal Proteins","Escherichia coli","Peptidoglycan","Escherichia coli Proteins"],"keywords":["FtsZ","MreB","Cell division","Peptidoglycan","Cell biology","Biology","Bacterial cell structure","Escherichia coli","Nucleoid","Cell","Chlamydia trachomatis","Cytoskeleton","Microbiology","Bacteria","Genetics","Virology","Gene","Chlamydia","Cell Shape","Rodz","Escherichia coli Proteins","QR1-502","Cytoskeletal Proteins","Bacterial Proteins","Cell Wall","Research Article"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. 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