{"doi":"10.3389/fmicb.2023.1171376","title":"Nucleotide-dependent activities of FtsA regulate the early establishment of a functional divisome during the Escherichia coli cell cycle","abstract":"During cell division in Escherichia coli , the highly conserved tubulin homolog FtsZ polymerizes and assembles into a ring-like structure, called the Z-ring, at the site of septation. For recruitment to the membrane surface, FtsZ polymers directly interact with membrane-associated proteins, predominantly FtsA in E. coli . FtsA shares structural homology with actin and, like actin, hydrolyzes ATP. Yeast actin detects nucleotide occupancy through a sensor region adjacent to the nucleotide binding site and adopts distinct conformations in monomeric and filamentous actin. Bacterial actin homologs also display considerable conformational flexibility across different nucleotide-bound states and polymerize. Here, we show that several amino acid residues proximal to the nucleotide binding site in FtsA are critical for function in vitro and in vivo . Each of these residues are important for ATP hydrolysis, phospholipid (PL) binding, ATP-dependent vesicle remodeling, and recruitment to the divisome in vivo , to varying degrees. Notably, we observed that Ser 84 and Glu 14 are essential for ATP-dependent vesicle remodeling and magnesium-dependent membrane release of FtsA from vesicles in vitro , and these defects likely underlie the loss of function by FtsA(E14R) and FtsA(S84L) in vivo . Finally, we demonstrate that FtsA(A188V), which is associated with temperature-sensitive growth in vivo , is defective for rapid ATP hydrolysis and ATP-dependent remodeling of PL vesicles in vitro . Together, our results show that loss of nucleotide-dependent activities by FtsA, such as ATP hydrolysis, membrane binding and release, and, most importantly, ATP-dependent PL remodeling, lead to failed Z-ring assembly and division defects in cells.","journal":"Frontiers in Microbiology","year":2023,"id":378647,"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":2,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9505,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2023-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":579439,"name":"Colby N. Ferreira","orcid":"0000-0001-6069-6191","position":1,"is_corresponding":false},{"id":1000634,"name":"Evelyn M. Siler","orcid":null,"position":2,"is_corresponding":false},{"id":854799,"name":"Katie Nelson","orcid":"0009-0009-7770-4253","position":3,"is_corresponding":false},{"id":580044,"name":"Catherine E. Trebino","orcid":null,"position":4,"is_corresponding":false},{"id":584562,"name":"Benjamin Piraino","orcid":"0000-0003-0823-9844","position":5,"is_corresponding":false},{"id":579442,"name":"Jodi L. Camberg","orcid":"0000-0002-8838-4461","position":6,"is_corresponding":false},{"id":579440,"name":"Josiah J. Morrison","orcid":"0000-0003-3294-8050","position":0,"is_corresponding":true}],"reference_count":27,"raw_metadata":null,"created_at":"2026-07-19T01:16:48.594070Z","pmid":"37250038","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":[]}