{"doi":"10.1128/mbio.00022-14","title":"ZapE Is a Novel Cell Division Protein Interacting with FtsZ and Modulating the Z-Ring Dynamics","abstract":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            Bacterial cell division requires the formation of a mature divisome complex positioned at the midcell. The localization of the divisome complex is determined by the correct positioning, assembly, and constriction of the FtsZ ring (Z-ring). Z-ring constriction control remains poorly understood and (to some extent) controversial, probably due to the fact that this phenomenon is transient and controlled by numerous factors. Here, we characterize ZapE, a novel ATPase found in Gram-negative bacteria, which is required for growth under conditions of low oxygen, while loss of\n            <jats:italic>zapE</jats:italic>\n            results in temperature-dependent elongation of cell shape. We found that ZapE is recruited to the Z-ring during late stages of the cell division process and correlates with constriction of the Z-ring. Overexpression or inactivation of\n            <jats:italic>zapE</jats:italic>\n            leads to elongation of\n            <jats:named-content content-type=\"genus-species\">Escherichia coli</jats:named-content>\n            and affects the dynamics of the Z-ring during division.\n            <jats:italic>In vitro</jats:italic>\n            , ZapE destabilizes FtsZ polymers in an ATP-dependent manner.\n          </jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE</jats:bold>\n            Bacterial cell division has mainly been characterized\n            <jats:italic>in vitro</jats:italic>\n            . In this report, we could identify ZapE as a novel cell division protein which is not essential\n            <jats:italic>in vitro</jats:italic>\n            but is required during an infectious process. The bacterial cell division process relies on the assembly, positioning, and constriction of FtsZ ring (the so-called Z-ring). Among nonessential cell division proteins recently identified, ZapE is the first in which detection at the Z-ring correlates with its constriction. We demonstrate that ZapE abundance has to be tightly regulated to allow cell division to occur; absence or overexpression of ZapE leads to bacterial filamentation. As\n            <jats:italic>zapE</jats:italic>\n            is not essential, we speculate that additional Z-ring destabilizing proteins transiently recruited during late cell division process might be identified in the future.\n          </jats:p>","journal":"mBio","year":2014,"id":621368,"datarank":0.637274286307404,"base_score":4.248495242049359,"endowment":4.248495242049359,"self_citation_contribution":0.637274286307404,"citation_network_contribution":0.0,"self_endowment_contribution":0.637274286307404,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":69,"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":1604426,"name":"Gouzel Karimova","orcid":null,"position":1,"is_corresponding":false},{"id":1604428,"name":"Andrew K. Fenton","orcid":"0000-0003-4042-4580","position":2,"is_corresponding":false},{"id":292386,"name":"Anastasia D. Gazi","orcid":"0000-0002-2922-3625","position":3,"is_corresponding":false},{"id":1604431,"name":"Nicholas West","orcid":null,"position":4,"is_corresponding":false},{"id":1604433,"name":"Lhousseine Touqui","orcid":null,"position":5,"is_corresponding":false},{"id":1604434,"name":"Marie-Christine Prevost","orcid":null,"position":6,"is_corresponding":false},{"id":120828,"name":"Jean-Michel Betton","orcid":null,"position":7,"is_corresponding":false},{"id":1604437,"name":"Oemer Poyraz","orcid":null,"position":8,"is_corresponding":false},{"id":1604439,"name":"Daniel Ladant","orcid":null,"position":9,"is_corresponding":false},{"id":1604440,"name":"Kenn Gerdes","orcid":null,"position":10,"is_corresponding":false},{"id":1604441,"name":"Philippe J. Sansonetti","orcid":null,"position":11,"is_corresponding":false},{"id":294747,"name":"Christoph M. Tang","orcid":"0000-0001-8366-3245","position":12,"is_corresponding":false},{"id":1604424,"name":"Benoit S. Marteyn","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"ZapE Is a Novel Cell Division Protein Interacting with FtsZ and Modulating the Z-Ring Dynamics","abstract":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            Bacterial cell division requires the formation of a mature divisome complex positioned at the midcell. The localization of the divisome complex is determined by the correct positioning, assembly, and constriction of the FtsZ ring (Z-ring). Z-ring constriction control remains poorly understood and (to some extent) controversial, probably due to the fact that this phenomenon is transient and controlled by numerous factors. Here, we characterize ZapE, a novel ATPase found in Gram-negative bacteria, which is required for growth under conditions of low oxygen, while loss of\n            <jats:italic>zapE</jats:italic>\n            results in temperature-dependent elongation of cell shape. We found that ZapE is recruited to the Z-ring during late stages of the cell division process and correlates with constriction of the Z-ring. Overexpression or inactivation of\n            <jats:italic>zapE</jats:italic>\n            leads to elongation of\n            <jats:named-content content-type=\"genus-species\">Escherichia coli</jats:named-content>\n            and affects the dynamics of the Z-ring during division.\n            <jats:italic>In vitro</jats:italic>\n            , ZapE destabilizes FtsZ polymers in an ATP-dependent manner.\n          </jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE</jats:bold>\n            Bacterial cell division has mainly been characterized\n            <jats:italic>in vitro</jats:italic>\n            . In this report, we could identify ZapE as a novel cell division protein which is not essential\n            <jats:italic>in vitro</jats:italic>\n            but is required during an infectious process. The bacterial cell division process relies on the assembly, positioning, and constriction of FtsZ ring (the so-called Z-ring). Among nonessential cell division proteins recently identified, ZapE is the first in which detection at the Z-ring correlates with its constriction. We demonstrate that ZapE abundance has to be tightly regulated to allow cell division to occur; absence or overexpression of ZapE leads to bacterial filamentation. As\n            <jats:italic>zapE</jats:italic>\n            is not essential, we speculate that additional Z-ring destabilizing proteins transiently recruited during late cell division process might be identified in the future.\n          </jats:p>","is_dataset_classified":null,"base_score":4.248495242049359,"endowment":4.248495242049359,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24595368","pmcid":"PMC3958796","openalex_id":"https://openalex.org/W2117941118","authors":[],"funders":[{"funder_name":"Wellcome Trust","grant_id":"102908","title":null},{"funder_name":"European Research Council","grant_id":"272398","title":null},{"funder_name":"European Commission","grant_id":"232798","title":"Homeostasis and rupture of the gut epithelium in the presence of commensals and pathogens"},{"funder_name":"European Commission","grant_id":"222720","title":"Molecular Targets Open for Regulation by the gut flora – New Avenues for improved Diet to Optimize European health"}],"total_grants":4,"fwci":3.4095,"citation_percentile":0.92703666,"influential_citations":0,"citation_trend":[{"year":2015,"count":4},{"year":2016,"count":6},{"year":2017,"count":6},{"year":2018,"count":4},{"year":2019,"count":2},{"year":2020,"count":12},{"year":2021,"count":5},{"year":2022,"count":6},{"year":2023,"count":10},{"year":2024,"count":7},{"year":2025,"count":6},{"year":2026,"count":1}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.1128/mbio.00022-14","host_type":"journal"},{"url":"https://doi.org/10.1128/mbio.00022-14","host_type":"publisher"},{"url":"https://journals.asm.org/doi/pdf/10.1128/mBio.00022-14","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24595368","host_type":"repository"},{"url":"http://citeseerx.ist.psu.edu/viewdoc/summary?doi=10.1.1.798.2980","host_type":""},{"url":"https://doaj.org/article/09defa5ffaca4dcfae9eb606c7f4b51b","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/3958796","host_type":"repository"},{"url":"https://ora.ox.ac.uk/objects/uuid:ca2fb63a-85a6-42c8-919b-3e9b178e46be","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC3958796","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC3958796?pdf=render","host_type":"Europe_PMC"},{"url":"http://dx.doi.org/10.1128/mBio.00022-14","host_type":""},{"url":"https://api.library.uq.edu.au/view/UQ:341166","host_type":""},{"url":"https://espace.library.uq.edu.au/view/UQ:341166","host_type":""},{"url":"https://dx.doi.org/10.1128/mbio.00022-14","host_type":""},{"url":"https://eprints.whiterose.ac.uk/id/eprint/161141/","host_type":""},{"url":"https://publications.scilifelab.se/publication/15ae34c421fc4ad49bd6fb20eb803581","host_type":""},{"url":"https://doi.org/https://doi.org/10.1128/mBio.00022-14","host_type":""}],"fields_of_study":["Bacterial Genetics and Biotechnology","Enzyme Structure and Function","Protein Structure and Dynamics","0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":["Adenosine Triphosphatases","Bacterial Proteins","Cell Division","Cytoskeletal Proteins","Escherichia coli","Protein Binding","Protein Interaction Mapping","Escherichia coli Proteins"],"keywords":["FtsZ","Cell division","Cell biology","Cell","Ring (chemistry)","Bacterial cell structure","Elongation","Biology","Division ring","Cytokinesis","Chemistry","Division (mathematics)","Bacteria","Biochemistry","Genetics","Materials science","Adenosine Triphosphatases","MICROBIOLOGY","Escherichia coli Proteins","2404 Microbiology","540","QR1-502","Cytoskeletal Proteins","Bacterial Proteins","Protein Interaction Mapping","2406 Virology","Escherichia coli","Research Article","Protein Binding"],"sdg_mappings":[{"sdg_number":3,"sdg_label":"3. Good health"},{"sdg_number":13,"sdg_label":"13. Climate action"},{"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":"2026-08-03T14:16:08.329164Z","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":[]}