[{"publication":"Science","OA_type":"closed access","scopus_import":"1","acknowledgement":"We thank all members of the Loose lab at ISTA for helpful discussions; M. Kojic for critical reading of the manuscript; A. Herrero (Sevilla University) for sharing her extensive BACTH plasmid library and other plasmids, as well as cyanobacterial strains; T. Dagan and F. Nies (both Kiel University) for sharing cyanobacterial strains and plasmids and for valuable discussions; N. Sapay and A. Michon for providing the Amphipaseek code, which enabled us to perform our large-scale amphipathic helix screen of cyanobacterial CorR proteins; V.-V. Hodirnau for support in cryo-ET data collection; and J. Hansen for advice about cryo-EM data processing.\r\nThis work was supported by the Scientific Service Units (SSU) of ISTA through resources provided by the Imaging & Optics Facility (IOF), the Scientific Computing (SciComp), the Electron Microscopy Facility (EMF), and the Lab Support Facility (LSF). This work was funded by the European Union’s Horizon 2020 research and innovation program (Marie Skłodowska-Curie grant 101034413 to B.L.S.); the European Research Council (ERC) of the European Union (grant ActinID 101076260 to F.K.M.S.); the Swiss National Science Foundation (starting grant TMSGI3_226208 to G.L.W.); and the Jean-Jacques et Letitia Lopez-Loreta Foundation (G.L.W.).","ec_funded":1,"date_created":"2026-04-26T22:01:46Z","pmid":1,"day":"16","month":"04","article_processing_charge":"No","volume":392,"intvolume":"       392","project":[{"_id":"fc2ed2f7-9c52-11eb-aca3-c01059dda49c","grant_number":"101034413","name":"IST-BRIDGE: International postdoctoral program","call_identifier":"H2020"},{"name":"A molecular atlas of Actin filament IDentities in the cell motility machinery","grant_number":"101076260","_id":"bd980d18-d553-11ed-ba76-ceaa645c97eb"}],"title":"Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape","quality_controlled":"1","year":"2026","publication_status":"published","status":"public","type":"journal_article","article_type":"original","_id":"21762","publication_identifier":{"issn":["0036-8075"],"eissn":["1095-9203"]},"doi":"10.1126/science.aea6343","article_number":"eaea6343","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"orcid":"0000-0002-3461-5391","full_name":"Springstein, Benjamin L","last_name":"Springstein","first_name":"Benjamin L","id":"b4eb62ef-ac72-11ed-9503-ed3b4d66c083"},{"id":"305ab18b-dc7d-11ea-9b2f-b58195228ea2","last_name":"Javoor","first_name":"Manjunath","full_name":"Javoor, Manjunath","orcid":"0000-0003-2311-2112"},{"first_name":"Daniela","last_name":"Megrian","full_name":"Megrian, Daniela"},{"full_name":"Hajdu, Roman","last_name":"Hajdu","first_name":"Roman","id":"ffab949d-133f-11ed-8f02-94de21ace503"},{"last_name":"Hanke","first_name":"Dustin M.","full_name":"Hanke, Dustin M."},{"full_name":"Zens, Bettina","orcid":"0000-0002-9561-1239","id":"45FD126C-F248-11E8-B48F-1D18A9856A87","last_name":"Zens","first_name":"Bettina"},{"full_name":"Weiss, Gregor L.","last_name":"Weiss","first_name":"Gregor L."},{"id":"48AD8942-F248-11E8-B48F-1D18A9856A87","last_name":"Schur","first_name":"Florian Km","full_name":"Schur, Florian Km","orcid":"0000-0003-4790-8078"},{"id":"462D4284-F248-11E8-B48F-1D18A9856A87","first_name":"Martin","last_name":"Loose","full_name":"Loose, Martin","orcid":"0000-0001-7309-9724"}],"corr_author":"1","acknowledged_ssus":[{"_id":"Bio"},{"_id":"ScienComp"},{"_id":"EM-Fac"},{"_id":"LifeSc"}],"citation":{"chicago":"Springstein, Benjamin L, Manjunath Javoor, Daniela Megrian, Roman Hajdu, Dustin M. Hanke, Bettina Zens, Gregor L. Weiss, Florian KM Schur, and Martin Loose. “Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cell Shape.” <i>Science</i>. AAAS, 2026. <a href=\"https://doi.org/10.1126/science.aea6343\">https://doi.org/10.1126/science.aea6343</a>.","ieee":"B. L. Springstein <i>et al.</i>, “Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape,” <i>Science</i>, vol. 392, no. 6795. AAAS, 2026.","mla":"Springstein, Benjamin L., et al. “Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling Cell Shape.” <i>Science</i>, vol. 392, no. 6795, eaea6343, AAAS, 2026, doi:<a href=\"https://doi.org/10.1126/science.aea6343\">10.1126/science.aea6343</a>.","ista":"Springstein BL, Javoor M, Megrian D, Hajdu R, Hanke DM, Zens B, Weiss GL, Schur FK, Loose M. 2026. Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. Science. 392(6795), eaea6343.","apa":"Springstein, B. L., Javoor, M., Megrian, D., Hajdu, R., Hanke, D. M., Zens, B., … Loose, M. (2026). Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. <i>Science</i>. AAAS. <a href=\"https://doi.org/10.1126/science.aea6343\">https://doi.org/10.1126/science.aea6343</a>","short":"B.L. Springstein, M. Javoor, D. Megrian, R. Hajdu, D.M. Hanke, B. Zens, G.L. Weiss, F.K. Schur, M. Loose, Science 392 (2026).","ama":"Springstein BL, Javoor M, Megrian D, et al. Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape. <i>Science</i>. 2026;392(6795). doi:<a href=\"https://doi.org/10.1126/science.aea6343\">10.1126/science.aea6343</a>"},"language":[{"iso":"eng"}],"oa_version":"None","issue":"6795","publisher":"AAAS","date_published":"2026-04-16T00:00:00Z","date_updated":"2026-04-28T13:29:05Z","department":[{"_id":"MaLo"},{"_id":"FlSc"},{"_id":"GradSch"},{"_id":"EM-Fac"}],"abstract":[{"text":"Bacteria, like eukaryotes, use conserved cytoskeletal systems for intracellular organization. The plasmid-encoded ParMRC system forms actin-like filaments that segregate low–copy number plasmids. In multicellular cyanobacteria such as Anabaena sp., we found that a chromosomally encoded ParMR system has evolved into a cytoskeletal system named CorMR with a function in cell shape control rather than DNA segregation. Live-cell imaging, in vitro reconstitution, and cryo–electron microscopy revealed that CorM formed dynamically unstable, antiparallel double-stranded filaments that were recruited to the membrane by CorR through an amphipathic helix conserved in multicellular cyanobacteria. CorMR filaments were regulated by MinC, which excluded them from the poles and division plane. Comparative genomics indicated that the repurposing of ParMR and Min systems coevolved with cyanobacterial multicellularity, highlighting the evolutionary plasticity of cytoskeletal systems in bacteria.","lang":"eng"}],"external_id":{"pmid":["41990175"]}},{"month":"07","article_processing_charge":"Yes (in subscription journal)","title":"The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture","publication":"Nature Microbiology","date_created":"2026-07-12T22:02:19Z","acknowledgement":"We thank all members of the Bernhardt, Rudner, Navarro and Vettiger Laboratories for support and helpful conversations. We thank C. Genoud, J. Daraspe, A. Mucciolo and D. de Bellis at the Electron Microscopy Facility of the University of Lausanne and E. Jeanvoine for providing access to workstations for cryo-ET image processing; S. Sterling, C. Borsa, J. Podgorski, P. Vinh Dip, E. Brignole and A. Osherov at the MIT.nano cryo-EM facility, K. Song and C. Xu at the University of Massachusetts cryo-EM facility, and R. Walsh and Z. Li at the cryo-EM at Harvard Medical School facility for providing access to the cryo-EM microscopes and for all their help, advice and maintenance of cryo-EM equipment. AFM was performed at the Harvard University Center for Nanoscale Systems (CNS), a member of the National Nanotechnology Coordinated Infrastructure Network (NNCI), which is supported by the National Science Foundation under NSF award no. ECCS-2025158. We thank N. S. Colella for excellent advice on AFM data acquisition and analysis; the MicRoN imaging core at Harvard Medical School for excellent advice on live cell imaging and maintenance of fluorescence microscopes; B. Krautz for creating the cartoon illustrations (www.sciencecommunicated.com); and L. Miles and R. Aeschimann for assistance with strain construction. A.V. was supported by an EMBO long-term postdoctoral fellowship ALTF_89-2019, the Swiss National Science Foundation (SNSF) Postdoc.Mobility fellowship P500PB_203143. P.P.N. was a recipient of early postdoc.mobility and postdoc.mobility fellowships (P2BSP3_188112 and P400PB_199252). This work was also supported by funding from the National Institutes of Health (R35GM142553 to L.H.C. and R01AI083365 to T.G.B.), investigator funds from the Howard Hughes Medical Institute (T.G.B.), an SNSF project grant (320030-236243 to A.V.), an SNSF Starting Grant (TMSGI3_218251 to P.P.N.), an SNSF Project grant (320030-236069 to P.P.N), an SNSF SPARK grant (CRSK-3_237167 to P.P.N.), cryo-EM funds from the Faculty of Biology and Medicine at University of Lausanne to P.P.N. and the Foundation Pierre Mercier pour la Science (to P.P.N.).","OA_place":"publisher","OA_type":"hybrid","scopus_import":"1","day":"03","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"pmid":1,"has_accepted_license":"1","oa":1,"article_type":"original","doi":"10.1038/s41564-026-02403-6","publication_identifier":{"eissn":["2058-5276"]},"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1038/s41564-026-02403-6"}],"_id":"22269","das_tickbox":"1","supplementarymaterial":"yes","quality_controlled":"1","type":"journal_article","status":"public","publication_status":"epub_ahead","year":"2026","citation":{"chicago":"Navarro, Paula P., Andrea Vettiger, Roman Hajdu, Virly Y. Ananda, Alejandro López-Tavares, Ernst W. Schmid, Johannes C. Walter, Martin Loose, Luke H. Chao, and Thomas G. Bernhardt. “The Penicillin-Binding Protein PBP1b Fortifies the Escherichia Coli Division Site against Osmotic Rupture.” <i>Nature Microbiology</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41564-026-02403-6\">https://doi.org/10.1038/s41564-026-02403-6</a>.","ieee":"P. P. Navarro <i>et al.</i>, “The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture,” <i>Nature Microbiology</i>. Springer Nature, 2026.","mla":"Navarro, Paula P., et al. “The Penicillin-Binding Protein PBP1b Fortifies the Escherichia Coli Division Site against Osmotic Rupture.” <i>Nature Microbiology</i>, Springer Nature, 2026, doi:<a href=\"https://doi.org/10.1038/s41564-026-02403-6\">10.1038/s41564-026-02403-6</a>.","ista":"Navarro PP, Vettiger A, Hajdu R, Ananda VY, López-Tavares A, Schmid EW, Walter JC, Loose M, Chao LH, Bernhardt TG. 2026. The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture. Nature Microbiology.","apa":"Navarro, P. P., Vettiger, A., Hajdu, R., Ananda, V. Y., López-Tavares, A., Schmid, E. W., … Bernhardt, T. G. (2026). The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture. <i>Nature Microbiology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41564-026-02403-6\">https://doi.org/10.1038/s41564-026-02403-6</a>","ama":"Navarro PP, Vettiger A, Hajdu R, et al. The penicillin-binding protein PBP1b fortifies the Escherichia coli division site against osmotic rupture. <i>Nature Microbiology</i>. 2026. doi:<a href=\"https://doi.org/10.1038/s41564-026-02403-6\">10.1038/s41564-026-02403-6</a>","short":"P.P. Navarro, A. Vettiger, R. Hajdu, V.Y. Ananda, A. López-Tavares, E.W. Schmid, J.C. Walter, M. Loose, L.H. Chao, T.G. Bernhardt, Nature Microbiology (2026)."},"oa_version":"Published Version","language":[{"iso":"eng"}],"dataavailabilitystatement":"The data, plasmids and strains that support the findings of this study are available from the corresponding authors by request. Representative tomograms are deposited in EMDB: EMD-27479 (wild-type), EMD-53351 (∆ponB), EMD-53357(∆lpoB) and EMD-53363 (∆ponA). Corresponding raw movie frames and stacks of tilt series are deposited as EMPIAR-11090 (wild type), EMPIAR-13502 (∆ponB), EMPIAR-13513 (∆lpoB) and EMPIAR-13512 (∆ponA), and will be released upon publication. Other data related to this manuscript (for example, AFM, light microscopy, growth curves and so on) can be found on Zenodo at https://doi.org/10.5281/zenodo.20841819 (ref. 101). Source data are provided with this paper. Scripts used in this study were deposited on GitHub at https://github.com/NavarroVettiger/Navarro-et-al_2022 and https://github.com/virlyananda/EM-ImageProcessing.","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Paula P.","last_name":"Navarro","full_name":"Navarro, Paula P."},{"last_name":"Vettiger","first_name":"Andrea","full_name":"Vettiger, Andrea"},{"id":"ffab949d-133f-11ed-8f02-94de21ace503","last_name":"Hajdu","first_name":"Roman","full_name":"Hajdu, Roman"},{"full_name":"Ananda, Virly Y.","first_name":"Virly Y.","last_name":"Ananda"},{"last_name":"López-Tavares","first_name":"Alejandro","full_name":"López-Tavares, Alejandro"},{"last_name":"Schmid","first_name":"Ernst W.","full_name":"Schmid, Ernst W."},{"first_name":"Johannes C.","last_name":"Walter","full_name":"Walter, Johannes C."},{"orcid":"0000-0001-7309-9724","full_name":"Loose, Martin","last_name":"Loose","first_name":"Martin","id":"462D4284-F248-11E8-B48F-1D18A9856A87"},{"last_name":"Chao","first_name":"Luke H.","full_name":"Chao, Luke H."},{"full_name":"Bernhardt, Thomas G.","first_name":"Thomas G.","last_name":"Bernhardt"}],"researchdata_availability":"yes","department":[{"_id":"MaLo"},{"_id":"GradSch"}],"date_updated":"2026-07-13T09:22:49Z","abstract":[{"text":"The divisome apparatus synthesizes septal peptidoglycan (PG) during bacterial division. In Escherichia coli, the class A penicillin-binding protein (aPBP) called PBP1b has been implicated in division, but its role in the process has remained unclear. Here we show using in situ cryo-electron tomography, genetics and other imaging methods that PBP1b is required to produce a wedge-like density of PG at the division site and that loss of this structure weakens the division site, making it hypersusceptible to osmotic lysis. Surprisingly, the activator LpoB needed for general PBP1b function was not required for its role in division. Of the two PBP1b isoforms produced in cells, we show that the one with an extended cytoplasmic N terminus localizes to and functions at the division site, probably via recruitment by the FtsA component of the divisome. The conservation of aPBPs with extended cytoplasmic N termini suggests that other Gram-negative bacteria may use similar mechanisms for division site reinforcement.","lang":"eng"}],"external_id":{"pmid":["42399561"]},"ddc":["570"],"publisher":"Springer Nature","date_published":"2026-07-03T00:00:00Z"}]