{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T18:51:08Z","timestamp":1791312668761,"version":"4.3.1"},"update-to":[{"DOI":"10.1371\/journal.pgen.1012319","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T00:00:00Z","timestamp":1791244800000}}],"reference-count":53,"publisher":"Public Library of Science (PLoS)","issue":"9","license":[{"start":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T00:00:00Z","timestamp":1790553600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"name":"David Braley Centre for Antibiotic Discovery"}],"content-domain":{"domain":["www.plosgenetics.org"],"crossmark-restriction":false},"short-container-title":["PLoS Genet"],"abstract":"<jats:p>\n                    Bacterial cell division requires precise regulation of septal peptidoglycan (PG) synthesis by the essential SEDS-bPBP synthase FtsWI. Activation of FtsWI is thought to occur through an allosteric cascade initiated by the late-arriving divisome protein FtsN and transmitted via the FtsQ-FtsL-FtsB (FtsQLB) complex, but the molecular details of this process remain incompletely defined and differ across species. Here, using the conditional essentiality of\n                    <jats:italic>ftsN<\/jats:italic>\n                    in\n                    <jats:italic>Pseudomonas aeruginosa<\/jats:italic>\n                    , we identify substitutions in the non-enzymatic pedestal domain of FtsI that bypass the requirement for FtsN. These mutations restore cell division in \u0394\n                    <jats:italic>ftsN<\/jats:italic>\n                    cells, suppress dominant-negative phenotypes of activation-defective\n                    <jats:italic>ftsL<\/jats:italic>\n                    alleles, and reduce cell length in an otherwise wild-type background, demonstrating that they alter FtsWI regulation to overcome the requirement for stimulation by both FtsN and FtsQLB. Mapping these mutations onto the\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    FtsQLBWI structure reveals that they cluster on distinct surfaces of the pedestal domain. Because some of these substitutions have been identified in clinical\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    isolates with increased aztreonam resistance, we next asked whether these regulatory substitutions alter \u03b2-lactam susceptibility. Variants at the FtsI-FtsL interface modestly reduce susceptibility to multiple \u03b2-lactam antibiotics, whereas a variant on the opposite face of the pedestal domain produces striking FtsN-dependent hypersusceptibility to the same molecules. These findings show that the FtsI pedestal domain plays a central role in the regulation of FtsWI and reveal a previously unrecognized relationship between divisome regulation and \u03b2-lactam susceptibility. More broadly, our work identifies the pedestal domain as a regulatory hub that integrates multiple inputs controlling septal PG synthesis and highlights its potential relevance to \u03b2-lactam resistance in clinical\n                    <jats:italic>P. aeruginosa<\/jats:italic>\n                    isolates.\n                  <\/jats:p>","DOI":"10.1371\/journal.pgen.1012319","type":"journal-article","created":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T17:51:31Z","timestamp":1790617891000},"page":"e1012319","update-policy":"https:\/\/doi.org\/10.1371\/journal.pgen.corrections_policy","source":"Crossref","is-referenced-by-count":0,"title":["Altered regulation of septal peptidoglycan synthesis modulates \u03b2-lactam susceptibility in Pseudomonas aeruginosa"],"prefix":"10.1371","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1461-0999","authenticated-orcid":true,"given":"Jake","family":"Colautti","sequence":"first","affiliation":[{"name":"McMaster University","place":["Hamilton, Ontario, Canada"],"department":["Department of Biochemistry and Biomedical Sciences"]},{"name":"McMaster University","place":["Hamilton, Ontario, Canada"],"department":["Michael DeGroote Institute for Infectious Disease Research"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1870-2903","authenticated-orcid":true,"given":"Alexander C.","family":"Anderson","sequence":"additional","affiliation":[{"name":"McMaster University","place":["Hamilton, Ontario, Canada"],"department":["Department of Biochemistry and Biomedical Sciences"]},{"name":"McMaster University","place":["Hamilton, Ontario, Canada"],"department":["Michael DeGroote Institute for Infectious Disease Research"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0000-3748-0050","authenticated-orcid":true,"given":"Wyatt P. K.","family":"Clark","sequence":"additional","affiliation":[{"name":"McMaster University","place":["Hamilton, Ontario, Canada"],"department":["Department of Biochemistry and Biomedical Sciences"]},{"name":"McMaster University","place":["Hamilton, Ontario, Canada"],"department":["Michael DeGroote Institute for Infectious Disease Research"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4225-2690","authenticated-orcid":true,"given":"Lindsey S.","family":"Marmont","sequence":"additional","affiliation":[{"name":"McMaster University","place":["Hamilton, Ontario, Canada"],"department":["Department of Biochemistry and Biomedical Sciences"]},{"name":"McMaster University","place":["Hamilton, Ontario, Canada"],"department":["Michael DeGroote Institute for Infectious Disease 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