[{"publication_identifier":{"issn":["0028-0836"],"eissn":["1476-4687"]},"supplementarymaterial":"yes","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"oa_version":"Published Version","has_accepted_license":"1","day":"29","das_tickbox":"1","OA_place":"publisher","fulldoi":"https://doi.org/10.1038/s41586-025-09852-9","article_type":"original","researchdata_availability":"yes","author":[{"first_name":"Oleg","full_name":"Dmytrenko, Oleg","last_name":"Dmytrenko"},{"last_name":"Yuan","full_name":"Yuan, Biao","first_name":"Biao"},{"full_name":"Crosby, Kadin T.","last_name":"Crosby","first_name":"Kadin T."},{"last_name":"Krebel","full_name":"Krebel, Max","first_name":"Max"},{"full_name":"Chen, Xiye","last_name":"Chen","first_name":"Xiye"},{"first_name":"Jakub S.","last_name":"Nowak","full_name":"Nowak, Jakub S."},{"full_name":"Chramiec-Głąbik, Andrzej","last_name":"Chramiec-Głąbik","first_name":"Andrzej"},{"first_name":"Bamidele","last_name":"Filani","full_name":"Filani, Bamidele"},{"full_name":"Gribling-Burrer, Anne-Sophie","last_name":"Gribling-Burrer","first_name":"Anne-Sophie"},{"full_name":"van der Toorn, Wiep","last_name":"van der Toorn","first_name":"Wiep"},{"last_name":"von Kleist","full_name":"von Kleist, Max","first_name":"Max"},{"full_name":"Achmedov, Tatjana","last_name":"Achmedov","first_name":"Tatjana"},{"first_name":"Redmond P.","full_name":"Smyth, Redmond P.","last_name":"Smyth"},{"full_name":"Glatt, Sebastian","last_name":"Glatt","first_name":"Sebastian"},{"id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e","orcid":"0000-0003-0456-0753","first_name":"Jack Peter Kelly","last_name":"Bravo","full_name":"Bravo, Jack Peter Kelly"},{"first_name":"Dirk W.","last_name":"Heinz","full_name":"Heinz, Dirk W."},{"full_name":"Jackson, Ryan N.","last_name":"Jackson","first_name":"Ryan N."},{"first_name":"Chase L.","last_name":"Beisel","full_name":"Beisel, Chase L."}],"department":[{"_id":"JaBr"}],"abstract":[{"text":"In all domains of life, tRNAs mediate the transfer of genetic information from mRNAs to proteins. As their depletion suppresses translation and, consequently, viral replication, tRNAs represent long-standing and increasingly recognized targets of innate immunity1,2,3,4,5. Here we report Cas12a3 effector nucleases from type V CRISPR–Cas adaptive immune systems in bacteria that preferentially cleave tRNAs after recognition of target RNA. Cas12a3 orthologues belong to one of two previously unreported nuclease clades that exhibit RNA-mediated cleavage of non-target RNA, and are distinct from all other known type V systems. Through cell-based and biochemical assays and direct RNA sequencing, we demonstrate that recognition of a complementary target RNA by the CRISPR RNA triggers Cas12a3 to cleave the conserved 5′-CCA-3′ tail of diverse tRNAs to drive growth arrest and anti-phage defence. Cryogenic electron microscopy structures further revealed a distinct tRNA-loading domain that positions the tRNA tail in the RuvC active site of the nuclease. By designing synthetic reporters that mimic the tRNA acceptor stem and tail, we expanded the capacity of current CRISPR-based diagnostics for multiplexed RNA detection. Overall, these findings reveal widespread tRNA inactivation as a previously unrecognized CRISPR-based immune strategy that broadens the application space of the existing CRISPR toolbox.","lang":"eng"}],"article_processing_charge":"Yes (via OA deal)","year":"2026","publisher":"Springer Nature","PlanS_conform":"1","month":"01","file_date_updated":"2026-07-27T10:35:26Z","type":"journal_article","publication_status":"published","dataavailabilitystatement":"The Illumina-based PFS screen data and the direct RNA Nanopore sequencing reads have been deposited into the European Nucleotide Archive under accession code PRJEB88250 (https://www.ebi.ac.uk/ena/browser/view/PRJEB88250). Models and associated cryo-EM maps have been deposited into the Electron Microscopy Data Bank (EMD) and PDB databases with the following accession codes: Ba1Cas12a3 binary complex (EMD-52275; PDB: 9HLX); Ba1Cas12a3 ternary complex (EMD-52287; PDB: 9HM6); Ba1Cas12a3 quaternary complex at pre-cleavage state (EMD-52285; PDB: 9HM4); and Ba1Cas12a3 quaternary complex at post-cleavage state (EMD-52286; PDB: 9HM5). Raw gel images are included as Supplementary Fig. 1. Source data are provided with this paper.","date_published":"2026-01-29T00:00:00Z","status":"public","oa":1,"title":"RNA-triggered Cas12a3 cleaves tRNA tails to execute bacterial immunity","OA_type":"hybrid","license":"https://creativecommons.org/licenses/by/4.0/","scopus_import":"1","date_updated":"2026-07-27T10:36:28Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","volume":649,"_id":"20963","page":"1312-1321","publication":"Nature","file":[{"success":1,"checksum":"f6b40af573fc7c0c0195e1428b1d0143","creator":"dernst","access_level":"open_access","date_created":"2026-07-27T10:35:26Z","file_name":"2026_Nature_Dmytrenko.pdf","relation":"main_file","content_type":"application/pdf","file_id":"22415","file_size":28253320,"date_updated":"2026-07-27T10:35:26Z"}],"citation":{"ista":"Dmytrenko O, Yuan B, Crosby KT, Krebel M, Chen X, Nowak JS, Chramiec-Głąbik A, Filani B, Gribling-Burrer A-S, van der Toorn W, von Kleist M, Achmedov T, Smyth RP, Glatt S, Bravo JPK, Heinz DW, Jackson RN, Beisel CL. 2026. RNA-triggered Cas12a3 cleaves tRNA tails to execute bacterial immunity. Nature. 649, 1312–1321.","short":"O. Dmytrenko, B. Yuan, K.T. Crosby, M. Krebel, X. Chen, J.S. Nowak, A. Chramiec-Głąbik, B. Filani, A.-S. Gribling-Burrer, W. van der Toorn, M. von Kleist, T. Achmedov, R.P. Smyth, S. Glatt, J.P.K. Bravo, D.W. Heinz, R.N. Jackson, C.L. Beisel, Nature 649 (2026) 1312–1321.","mla":"Dmytrenko, Oleg, et al. “RNA-Triggered Cas12a3 Cleaves TRNA Tails to Execute Bacterial Immunity.” <i>Nature</i>, vol. 649, Springer Nature, 2026, pp. 1312–21, doi:<a href=\"https://doi.org/10.1038/s41586-025-09852-9\">10.1038/s41586-025-09852-9</a>.","ieee":"O. Dmytrenko <i>et al.</i>, “RNA-triggered Cas12a3 cleaves tRNA tails to execute bacterial immunity,” <i>Nature</i>, vol. 649. Springer Nature, pp. 1312–1321, 2026.","chicago":"Dmytrenko, Oleg, Biao Yuan, Kadin T. Crosby, Max Krebel, Xiye Chen, Jakub S. Nowak, Andrzej Chramiec-Głąbik, et al. “RNA-Triggered Cas12a3 Cleaves TRNA Tails to Execute Bacterial Immunity.” <i>Nature</i>. Springer Nature, 2026. <a href=\"https://doi.org/10.1038/s41586-025-09852-9\">https://doi.org/10.1038/s41586-025-09852-9</a>.","ama":"Dmytrenko O, Yuan B, Crosby KT, et al. RNA-triggered Cas12a3 cleaves tRNA tails to execute bacterial immunity. <i>Nature</i>. 2026;649:1312-1321. doi:<a href=\"https://doi.org/10.1038/s41586-025-09852-9\">10.1038/s41586-025-09852-9</a>","apa":"Dmytrenko, O., Yuan, B., Crosby, K. T., Krebel, M., Chen, X., Nowak, J. S., … Beisel, C. L. (2026). RNA-triggered Cas12a3 cleaves tRNA tails to execute bacterial immunity. <i>Nature</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41586-025-09852-9\">https://doi.org/10.1038/s41586-025-09852-9</a>"},"pmid":1,"external_id":{"pmid":["41501459"]},"date_created":"2026-01-08T07:57:17Z","acknowledgement":"We thank Ł. Koziej for processing of the initial cryo-EM datasets, S. Schmelz for support in cryo-EM, A. Gatzemeier for assistance in the purification of dBa1Cas12a3, R. Rarose for support with the in vitro RNA experiments, M. Kaminski for providing purified PsmCas13b protein, L. Schönemann for protein purification, and C. Krempl and S. Backesfor providing the RSV and influenza A transcript-encoding plasmids. This work was supported through funding by the European Research Council (101001394 to S.G.; 865973 and 101158249 to C.L.B.), the R. Gaurth Hansen Family (to R.N.J.), the National Institutes of Health (R35GM138080 to R.N.J.), the PostDoc Plus Program from the Graduate School of Life Sciences at Julius-Maximilians-Universität Würzburg (to O.D.), and the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy–The Berlin Mathematics Research Center MATH+ (EXC−2046/1, project ID: 390685689 to M.v.K.). Open access funding provided by Helmholtz-Zentrum für Infektionsforschung GmbH (HZI).","quality_controlled":"1","language":[{"iso":"eng"}],"doi":"10.1038/s41586-025-09852-9","ddc":["570"],"intvolume":"       649"},{"das_tickbox":"1","day":"10","oa_version":"None","publication_identifier":{"issn":["1931-3128"],"eissn":["1934-6069"]},"author":[{"first_name":"Daniel","id":"128eaab9-b327-11f0-bdbe-e02d5abac73b","last_name":"Williams-Jones","full_name":"Williams-Jones, Daniel"},{"full_name":"Bravo, Jack Peter Kelly","last_name":"Bravo","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e","first_name":"Jack Peter Kelly","orcid":"0000-0003-0456-0753"}],"department":[{"_id":"JaBr"}],"article_type":"original","fulldoi":"https://doi.org/10.1016/j.chom.2026.05.013","corr_author":"1","month":"06","publisher":"Elsevier","year":"2026","article_processing_charge":"No","abstract":[{"lang":"eng","text":"In this issue of Cell Host & Microbe, Osterman et al. discover aRES,1 a new family of bacterial immune proteins that deplete cellular NAD+, generating cleavage products that cannot be utilized by canonical phage NAD+ regeneration pathways. They identify the invader-specific trigger for aRES and characterize two distinct evolutionary countermeasures employed by phages to resist aRES."}],"project":[{"grant_number":"PAT1617625","name":"Search & Destroy: Mechanisms of anti-plasmid immunity","_id":"9f295cab-ad08-11f1-bc83-9e197d0f6d50"}],"date_published":"2026-06-10T00:00:00Z","status":"public","publication_status":"published","type":"journal_article","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","date_updated":"2026-09-16T07:35:26Z","scopus_import":"1","OA_type":"closed access","title":"NAD to the bone: How bacteria put phages under aRES-t … and how phages fight back","citation":{"ama":"Williams-Jones D, Bravo JPK. NAD to the bone: How bacteria put phages under aRES-t … and how phages fight back. <i>Cell Host &#38; Microbe</i>. 2026;34(6):978-980. doi:<a href=\"https://doi.org/10.1016/j.chom.2026.05.013\">10.1016/j.chom.2026.05.013</a>","chicago":"Williams-Jones, Daniel, and Jack Peter Kelly Bravo. “NAD to the Bone: How Bacteria Put Phages under ARES-t … and How Phages Fight Back.” <i>Cell Host &#38; Microbe</i>. Elsevier, 2026. <a href=\"https://doi.org/10.1016/j.chom.2026.05.013\">https://doi.org/10.1016/j.chom.2026.05.013</a>.","apa":"Williams-Jones, D., &#38; Bravo, J. P. K. (2026). NAD to the bone: How bacteria put phages under aRES-t … and how phages fight back. <i>Cell Host &#38; Microbe</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.chom.2026.05.013\">https://doi.org/10.1016/j.chom.2026.05.013</a>","short":"D. Williams-Jones, J.P.K. Bravo, Cell Host &#38; Microbe 34 (2026) 978–980.","ista":"Williams-Jones D, Bravo JPK. 2026. NAD to the bone: How bacteria put phages under aRES-t … and how phages fight back. Cell Host &#38; Microbe. 34(6), 978–980.","mla":"Williams-Jones, Daniel, and Jack Peter Kelly Bravo. “NAD to the Bone: How Bacteria Put Phages under ARES-t … and How Phages Fight Back.” <i>Cell Host &#38; Microbe</i>, vol. 34, no. 6, Elsevier, 2026, pp. 978–80, doi:<a href=\"https://doi.org/10.1016/j.chom.2026.05.013\">10.1016/j.chom.2026.05.013</a>.","ieee":"D. Williams-Jones and J. P. K. Bravo, “NAD to the bone: How bacteria put phages under aRES-t … and how phages fight back,” <i>Cell Host &#38; Microbe</i>, vol. 34, no. 6. Elsevier, pp. 978–980, 2026."},"publication":"Cell Host & Microbe","page":"978-980","volume":34,"_id":"21996","quality_controlled":"1","acknowledgement":"This work was supported by the Austrian Science Fund (FWF) (10.55776/PAT1617625).","date_created":"2026-06-14T22:01:42Z","issue":"6","external_id":{"pmid":["42269584"]},"pmid":1,"intvolume":"        34","doi":"10.1016/j.chom.2026.05.013","language":[{"iso":"eng"}]},{"month":"09","year":"2026","article_processing_charge":"Yes (via OA deal)","PlanS_conform":"1","publisher":"Wiley","project":[{"_id":"9f295cab-ad08-11f1-bc83-9e197d0f6d50","name":"Search & Destroy: Mechanisms of anti-plasmid immunity","grant_number":"PAT1617625"}],"abstract":[{"lang":"eng","text":"Argonaute proteins mediate RNA interference in eukaryotes and nucleic‐acid defence in prokaryotes. Although these systems operate in distinct biological contexts and produce diverse downstream outcomes, they share a conserved structural architecture and mechanism of guide‐dependent target recognition. Here, we argue that Argonautes function as programmable surveillance platforms that kinetically sample nucleic acids, engage targets through sequential pairing and conformational checkpoints, and couple recognition to functional outputs through regulated structural transitions. Rather than representing distinct recognition mechanisms, the diverse targeting behaviours observed across Argonaute families reflect different implementations of this shared framework, in which guide biogenesis, target accessibility, pairing requirements and effector coupling are weighted differently according to biological context. Viewing Argonautes through this common operational logic reconciles apparent differences in specificity, mismatch tolerance and target selection across systems, while providing a unified conceptual framework for understanding their evolution and guiding the engineering of programmable nucleic‐acid recognition technologies."}],"status":"public","date_published":"2026-09-08T00:00:00Z","publication_status":"epub_ahead","type":"journal_article","das_tickbox":"0","has_accepted_license":"1","day":"08","supplementarymaterial":"no","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"oa_version":"Published Version","publication_identifier":{"issn":["0014-5793"],"eissn":["1873-3468"]},"researchdata_availability":"no","department":[{"_id":"JaBr"}],"author":[{"last_name":"Bravo","full_name":"Bravo, Jack Peter Kelly","first_name":"Jack Peter Kelly","orcid":"0000-0003-0456-0753","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e"}],"article_type":"original","corr_author":"1","fulldoi":"https://doi.org/10.1002/1873-3468.70450","OA_place":"publisher","quality_controlled":"1","date_created":"2026-09-17T09:31:02Z","acknowledgement":"I would like to thank K. Kiernan and F. Alcon for insightful comments and feedback. We acknowledge support from ISTA and from the Austrian Science Fund (FWF) (10.55776/PAT1617625). The author used Claude (Anthropic) to assist with improving the clarity and readability of portions of the manuscript. All scientific content, interpretation and conclusions were conceived, verified and approved by the author, who takes full responsibility for the final manuscript. Open Access funding provided by Institute of Science and Technology Austria.","article_number":"1873-3468.70450","pmid":1,"external_id":{"pmid":["42711859"]},"ddc":["570"],"doi":"10.1002/1873-3468.70450","language":[{"iso":"eng"}],"main_file_link":[{"open_access":"1","url":"https://doi.org/10.1002/1873-3468.70450"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","scopus_import":"1","date_updated":"2026-09-17T11:48:51Z","title":"‘Guide and Prejudice’ -  How Argonautes recognize targets across domains of life","OA_type":"hybrid","oa":1,"citation":{"ama":"Bravo JPK. ‘Guide and Prejudice’ -  How Argonautes recognize targets across domains of life. <i>FEBS Letters</i>. 2026. doi:<a href=\"https://doi.org/10.1002/1873-3468.70450\">10.1002/1873-3468.70450</a>","chicago":"Bravo, Jack Peter Kelly. “‘Guide and Prejudice’ -  How Argonautes Recognize Targets across Domains of Life.” <i>FEBS Letters</i>. Wiley, 2026. <a href=\"https://doi.org/10.1002/1873-3468.70450\">https://doi.org/10.1002/1873-3468.70450</a>.","apa":"Bravo, J. P. K. (2026). ‘Guide and Prejudice’ -  How Argonautes recognize targets across domains of life. <i>FEBS Letters</i>. Wiley. <a href=\"https://doi.org/10.1002/1873-3468.70450\">https://doi.org/10.1002/1873-3468.70450</a>","short":"J.P.K. Bravo, FEBS Letters (2026).","ista":"Bravo JPK. 2026. ‘Guide and Prejudice’ -  How Argonautes recognize targets across domains of life. FEBS Letters., 1873–3468.70450.","ieee":"J. P. K. Bravo, “‘Guide and Prejudice’ -  How Argonautes recognize targets across domains of life,” <i>FEBS Letters</i>. Wiley, 2026.","mla":"Bravo, Jack Peter Kelly. “‘Guide and Prejudice’ -  How Argonautes Recognize Targets across Domains of Life.” <i>FEBS Letters</i>, 1873–3468.70450, Wiley, 2026, doi:<a href=\"https://doi.org/10.1002/1873-3468.70450\">10.1002/1873-3468.70450</a>."},"publication":"FEBS Letters","_id":"22941"},{"article_type":"comment","department":[{"_id":"JaBr"}],"author":[{"last_name":"Bravo","full_name":"Bravo, Jack Peter Kelly","first_name":"Jack Peter Kelly","orcid":"0000-0003-0456-0753","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e"}],"researchdata_availability":"no","fulldoi":"https://doi.org/10.1126/science.ael0758","corr_author":"1","day":"17","das_tickbox":"0","publication_identifier":{"issn":["0036-8075"],"eissn":["1095-9203"]},"oa_version":"None","supplementarymaterial":"no","publication_status":"published","date_published":"2026-09-17T00:00:00Z","status":"public","type":"journal_article","month":"09","abstract":[{"text":"Ancient viral warfare could be at the root of modern class 1 CRISPR bacterial defense systems","lang":"eng"}],"publisher":"AAAS","article_processing_charge":"No","year":"2026","publication":"Science","citation":{"mla":"Bravo, Jack Peter Kelly. “A Viral Origin for RNA-Guided Immunity.” <i>Science</i>, vol. 393, no. 6817, AAAS, 2026, pp. 1187–88, doi:<a href=\"https://doi.org/10.1126/science.ael0758\">10.1126/science.ael0758</a>.","ieee":"J. P. K. Bravo, “A viral origin for RNA-guided immunity,” <i>Science</i>, vol. 393, no. 6817. AAAS, pp. 1187–1188, 2026.","short":"J.P.K. Bravo, Science 393 (2026) 1187–1188.","ista":"Bravo JPK. 2026. A viral origin for RNA-guided immunity. Science. 393(6817), 1187–1188.","apa":"Bravo, J. P. K. (2026). A viral origin for RNA-guided immunity. <i>Science</i>. AAAS. <a href=\"https://doi.org/10.1126/science.ael0758\">https://doi.org/10.1126/science.ael0758</a>","ama":"Bravo JPK. A viral origin for RNA-guided immunity. <i>Science</i>. 2026;393(6817):1187-1188. doi:<a href=\"https://doi.org/10.1126/science.ael0758\">10.1126/science.ael0758</a>","chicago":"Bravo, Jack Peter Kelly. “A Viral Origin for RNA-Guided Immunity.” <i>Science</i>. AAAS, 2026. <a href=\"https://doi.org/10.1126/science.ael0758\">https://doi.org/10.1126/science.ael0758</a>."},"_id":"23000","volume":393,"page":"1187-1188","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","OA_type":"closed access","title":"A viral origin for RNA-guided immunity","date_updated":"2026-10-07T08:10:18Z","scopus_import":"1","intvolume":"       393","language":[{"iso":"eng"}],"doi":"10.1126/science.ael0758","date_created":"2026-09-27T22:01:52Z","quality_controlled":"1","external_id":{"pmid":["42752153"]},"pmid":1,"issue":"6817"},{"scopus_import":"1","date_updated":"2025-07-03T11:58:22Z","oa":1,"title":"DNA targeting by compact Cas9d and its resurrected ancestor","OA_type":"gold","DOAJ_listed":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","volume":16,"_id":"18848","citation":{"mla":"Ocampo, Rodrigo Fregoso, et al. “DNA Targeting by Compact Cas9d and Its Resurrected Ancestor.” <i>Nature Communications</i>, vol. 16, 457, Springer Nature, 2025, doi:<a href=\"https://doi.org/10.1038/s41467-024-55573-4\">10.1038/s41467-024-55573-4</a>.","ieee":"R. F. Ocampo <i>et al.</i>, “DNA targeting by compact Cas9d and its resurrected ancestor,” <i>Nature Communications</i>, vol. 16. Springer Nature, 2025.","short":"R.F. Ocampo, J.P.K. Bravo, T.L. Dangerfield, I. Nocedal, S.A. Jirde, L.M. Alexander, N.C. Thomas, A. Das, S. Nielson, K.A. Johnson, C.T. Brown, C.N. Butterfield, D.S.A. Goltsman, D.W. Taylor, Nature Communications 16 (2025).","ista":"Ocampo RF, Bravo JPK, Dangerfield TL, Nocedal I, Jirde SA, Alexander LM, Thomas NC, Das A, Nielson S, Johnson KA, Brown CT, Butterfield CN, Goltsman DSA, Taylor DW. 2025. DNA targeting by compact Cas9d and its resurrected ancestor. Nature Communications. 16, 457.","apa":"Ocampo, R. F., Bravo, J. P. K., Dangerfield, T. L., Nocedal, I., Jirde, S. A., Alexander, L. M., … Taylor, D. W. (2025). DNA targeting by compact Cas9d and its resurrected ancestor. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-024-55573-4\">https://doi.org/10.1038/s41467-024-55573-4</a>","ama":"Ocampo RF, Bravo JPK, Dangerfield TL, et al. DNA targeting by compact Cas9d and its resurrected ancestor. <i>Nature Communications</i>. 2025;16. doi:<a href=\"https://doi.org/10.1038/s41467-024-55573-4\">10.1038/s41467-024-55573-4</a>","chicago":"Ocampo, Rodrigo Fregoso, Jack Peter Kelly Bravo, Tyler L. Dangerfield, Isabel Nocedal, Samatar A. Jirde, Lisa M. Alexander, Nicole C. Thomas, et al. “DNA Targeting by Compact Cas9d and Its Resurrected Ancestor.” <i>Nature Communications</i>. Springer Nature, 2025. <a href=\"https://doi.org/10.1038/s41467-024-55573-4\">https://doi.org/10.1038/s41467-024-55573-4</a>."},"file":[{"file_size":5450660,"file_id":"18869","content_type":"application/pdf","relation":"main_file","file_name":"2025_NatureComm_Ocampo.pdf","date_updated":"2025-01-22T14:35:22Z","date_created":"2025-01-22T14:35:22Z","access_level":"open_access","checksum":"885e96690620790d5c9f188a1587b4cd","creator":"dernst","success":1}],"publication":"Nature Communications","article_number":"457","pmid":1,"external_id":{"pmid":["39774105"]},"quality_controlled":"1","date_created":"2025-01-19T23:01:50Z","acknowledgement":"We would like to thank M. Ocampo Camacho and M.F. Canedo Ocampo for assistance with the figures. We thank M. Hooper for assistance developing the GFP assay and operating the CE machine for in vitro cleavage analysis. We thank E. Schwartz and A. Brilot for expert cryo-EM support in the Sauer Structural Biology Laboratory at UT Austin. This work was funded, in part, by a sponsored research agreement with Metagenomi, Inc. (to D.W.T), a Welch Foundation Research Grant F-1938 (to D.W.T), and the Robert J. Kleberg, Jr. and Helen C. Kleberg Foundation Medical Research Grant (to D.W.T), and a grant from the National Institute of Allergy and Infectious Diseases (NIAID 1R01AI110577 to K.A.J.).","doi":"10.1038/s41467-024-55573-4","language":[{"iso":"eng"}],"intvolume":"        16","ddc":["570"],"oa_version":"Published Version","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"publication_identifier":{"eissn":["2041-1723"]},"has_accepted_license":"1","day":"07","fulldoi":"https://doi.org/10.1038/s41467-024-55573-4","OA_place":"publisher","author":[{"first_name":"Rodrigo Fregoso","full_name":"Ocampo, Rodrigo Fregoso","last_name":"Ocampo"},{"full_name":"Bravo, Jack Peter Kelly","last_name":"Bravo","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e","first_name":"Jack Peter Kelly","orcid":"0000-0003-0456-0753"},{"full_name":"Dangerfield, Tyler L.","last_name":"Dangerfield","first_name":"Tyler L."},{"first_name":"Isabel","full_name":"Nocedal, Isabel","last_name":"Nocedal"},{"full_name":"Jirde, Samatar A.","last_name":"Jirde","first_name":"Samatar A."},{"last_name":"Alexander","full_name":"Alexander, Lisa M.","first_name":"Lisa M."},{"full_name":"Thomas, Nicole C.","last_name":"Thomas","first_name":"Nicole C."},{"first_name":"Anjali","full_name":"Das, Anjali","last_name":"Das"},{"full_name":"Nielson, Sarah","last_name":"Nielson","first_name":"Sarah"},{"first_name":"Kenneth A.","last_name":"Johnson","full_name":"Johnson, Kenneth A."},{"first_name":"Christopher T.","last_name":"Brown","full_name":"Brown, Christopher T."},{"first_name":"Cristina N.","last_name":"Butterfield","full_name":"Butterfield, Cristina N."},{"full_name":"Goltsman, Daniela S.A.","last_name":"Goltsman","first_name":"Daniela S.A."},{"first_name":"David W.","full_name":"Taylor, David W.","last_name":"Taylor"}],"department":[{"_id":"JaBr"}],"article_type":"original","article_processing_charge":"Yes","year":"2025","publisher":"Springer Nature","abstract":[{"lang":"eng","text":"Type II CRISPR endonucleases are widely used programmable genome editing tools. Recently, CRISPR-Cas systems with highly compact nucleases have been discovered, including Cas9d (a type II-D nuclease). Here, we report the cryo-EM structures of a Cas9d nuclease (747 amino acids in length) in multiple functional states, revealing a stepwise process of DNA targeting involving a conformational switch in a REC2 domain insertion. Our structures provide insights into the intricately folded guide RNA which acts as a structural scaffold to anchor small, flexible protein domains for DNA recognition. The sgRNA can be truncated by up to ~25% yet still retain activity in vivo. Using ancestral sequence reconstruction, we generated compact nucleases capable of efficient genome editing in mammalian cells. Collectively, our results provide mechanistic insights into the evolution and DNA targeting of diverse type II CRISPR-Cas systems, providing a blueprint for future re-engineering of minimal RNA-guided DNA endonucleases."}],"month":"01","type":"journal_article","file_date_updated":"2025-01-22T14:35:22Z","date_published":"2025-01-07T00:00:00Z","status":"public","publication_status":"published"},{"acknowledgement":"We thank Rotem Sorek (Weizmann Institute of Science) for the Lambda Gam mutant and Ian Molineux (University of Texas) for T4Δgp2. We thank You Yu (Zhejiang University-University of Edinburgh Institute) and J. De La Cruz (MSK) for assistance with cryo-EM data collection and Lyuqin Zheng (MSK) for discussions on structural analysis. We thank the Imaging and Microscopy Centre (IMC) at the University of Southampton. This work was supported by Royal Society grant RGS\\R2\\222312 to F.L.N.; Welch Foundation grant F-1938 and National Institutes of Health R35GM138348 to D.W.T.; Wessex Medical Research Innovation grant AE06 to T.A.; and NIH grant GM145888 and Maloris Foundation and Memorial Sloan-Kettering Core grant (P30-CA008748) to D.J.P. In addition to MSKCC cryo-EM resources, some of this work was performed at the National Center for CryoEM Access and Training (NCCAT) and the Simons Electron Microscopy Center located at the New York Structural Biology Center, supported by the NIH Common Fund Transformative High Resolution Cryo-Electron Microscopy program (U24 GM129539) and Simons Foundation (SF349247) and NY State Assembly grants. This research used NSLS-II MX X-ray User Resources (FMX) of the National Synchrotron Light Source II, operated for the DOE Office of Science by Brookhaven National Laboratory under contract no. DE-SC0012704. The Center for BioMolecular Structure (CBMS) is primarily supported by the NIH, the National Institute of General Medical Sciences (NIGMS) through a Center Core P30 Grant (P30GM133893), and by the DOE Office of Biological and Environmental Research (KP1605010). R.K. and E.V.K. are supported by the Intramural Research Program of the NIH (National Library of Medicine).","date_created":"2025-08-07T05:00:04Z","quality_controlled":"1","pmid":1,"external_id":{"pmid":["40730155"],"isi":["001603560700005"]},"issue":"21","ddc":["570"],"intvolume":"       188","isi":1,"language":[{"iso":"eng"}],"doi":"10.1016/j.cell.2025.07.002","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Kiwa is a membrane-embedded defense supercomplex activated at phage attachment sites","OA_type":"hybrid","oa":1,"scopus_import":"1","date_updated":"2025-12-29T14:15:58Z","publication":"Cell","file":[{"file_name":"2025_Cell_Zhang.pdf","content_type":"application/pdf","relation":"main_file","file_id":"20875","file_size":32104588,"date_updated":"2025-12-29T14:15:25Z","access_level":"open_access","date_created":"2025-12-29T14:15:25Z","checksum":"b944de5fbd7455f58e1ff338ad352239","creator":"dernst","success":1}],"citation":{"mla":"Zhang, Zhiying, et al. “Kiwa Is a Membrane-Embedded Defense Supercomplex Activated at Phage Attachment Sites.” <i>Cell</i>, vol. 188, no. 21, Elsevier, 2025, p. 5862–5877.e23, doi:<a href=\"https://doi.org/10.1016/j.cell.2025.07.002\">10.1016/j.cell.2025.07.002</a>.","ieee":"Z. Zhang <i>et al.</i>, “Kiwa is a membrane-embedded defense supercomplex activated at phage attachment sites,” <i>Cell</i>, vol. 188, no. 21. Elsevier, p. 5862–5877.e23, 2025.","ista":"Zhang Z, Todeschini TC, Wu Y, Kogay R, Naji A, Cardenas Rodriguez J, Mondi R, Kaganovich D, Taylor DW, Bravo JPK, Teplova M, Amen T, Koonin E, Patel DJ, Nobrega FL. 2025. Kiwa is a membrane-embedded defense supercomplex activated at phage attachment sites. Cell. 188(21), 5862–5877.e23.","short":"Z. Zhang, T.C. Todeschini, Y. Wu, R. Kogay, A. Naji, J. Cardenas Rodriguez, R. Mondi, D. Kaganovich, D.W. Taylor, J.P.K. Bravo, M. Teplova, T. Amen, E. Koonin, D.J. Patel, F.L. Nobrega, Cell 188 (2025) 5862–5877.e23.","apa":"Zhang, Z., Todeschini, T. C., Wu, Y., Kogay, R., Naji, A., Cardenas Rodriguez, J., … Nobrega, F. L. (2025). Kiwa is a membrane-embedded defense supercomplex activated at phage attachment sites. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2025.07.002\">https://doi.org/10.1016/j.cell.2025.07.002</a>","chicago":"Zhang, Zhiying, Thomas C. Todeschini, Yi Wu, Roman Kogay, Ameena Naji, Joaquin Cardenas Rodriguez, Rupavidhya Mondi, et al. “Kiwa Is a Membrane-Embedded Defense Supercomplex Activated at Phage Attachment Sites.” <i>Cell</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.cell.2025.07.002\">https://doi.org/10.1016/j.cell.2025.07.002</a>.","ama":"Zhang Z, Todeschini TC, Wu Y, et al. Kiwa is a membrane-embedded defense supercomplex activated at phage attachment sites. <i>Cell</i>. 2025;188(21):5862-5877.e23. doi:<a href=\"https://doi.org/10.1016/j.cell.2025.07.002\">10.1016/j.cell.2025.07.002</a>"},"_id":"20143","volume":188,"page":"5862-5877.e23","month":"10","abstract":[{"text":"Bacteria and archaea deploy diverse antiviral defense systems, many of which remain mechanistically uncharacterized. Here, we characterize Kiwa, a widespread two-component system composed of the transmembrane sensor KwaA and the DNA-binding effector KwaB. Cryogenic electron microscopy (cryo-EM) analysis reveals that KwaA and KwaB assemble into a large, membrane-associated supercomplex. Upon phage binding, KwaA senses infection at the membrane, leading to KwaB binding of ejected phage DNA and inhibition of replication and late transcription, without inducing host cell death. Although KwaB can bind DNA independently, its antiviral activity requires association with KwaA, suggesting spatial or conformational regulation. We show that the phage-encoded DNA-mimic protein Gam directly binds and inhibits KwaB but that co-expression with the Gam-targeted RecBCD system restores protection by Kiwa. Our findings support a model in which Kiwa coordinates membrane-associated detection of phage infection with downstream DNA binding by its effector, forming a spatially coordinated antiviral mechanism.","lang":"eng"}],"year":"2025","article_processing_charge":"Yes (in subscription journal)","publisher":"Elsevier","PlanS_conform":"1","publication_status":"published","status":"public","date_published":"2025-10-16T00:00:00Z","file_date_updated":"2025-12-29T14:15:25Z","type":"journal_article","day":"16","has_accepted_license":"1","publication_identifier":{"issn":["0092-8674"],"eissn":["1097-4172"]},"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"oa_version":"Published Version","article_type":"original","department":[{"_id":"JaBr"}],"author":[{"full_name":"Zhang, Zhiying","last_name":"Zhang","first_name":"Zhiying"},{"first_name":"Thomas C.","last_name":"Todeschini","full_name":"Todeschini, Thomas C."},{"full_name":"Wu, Yi","last_name":"Wu","first_name":"Yi"},{"last_name":"Kogay","full_name":"Kogay, Roman","first_name":"Roman"},{"first_name":"Ameena","full_name":"Naji, Ameena","last_name":"Naji"},{"first_name":"Joaquin","full_name":"Cardenas Rodriguez, Joaquin","last_name":"Cardenas Rodriguez"},{"full_name":"Mondi, Rupavidhya","last_name":"Mondi","first_name":"Rupavidhya"},{"full_name":"Kaganovich, Daniel","last_name":"Kaganovich","first_name":"Daniel"},{"full_name":"Taylor, David W.","last_name":"Taylor","first_name":"David W."},{"last_name":"Bravo","full_name":"Bravo, Jack Peter Kelly","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e","first_name":"Jack Peter Kelly","orcid":"0000-0003-0456-0753"},{"full_name":"Teplova, Marianna","last_name":"Teplova","first_name":"Marianna"},{"first_name":"Triana","last_name":"Amen","full_name":"Amen, Triana"},{"last_name":"Koonin","full_name":"Koonin, Eugene","first_name":"Eugene"},{"first_name":"Dinshaw J.","full_name":"Patel, Dinshaw J.","last_name":"Patel"},{"first_name":"Franklin L.","last_name":"Nobrega","full_name":"Nobrega, Franklin L."}],"OA_place":"publisher","fulldoi":"https://doi.org/10.1016/j.cell.2025.07.002"},{"year":"2024","article_processing_charge":"Yes","publisher":"Springer Nature","abstract":[{"lang":"eng","text":"CRISPR-Cas9 is a powerful tool for genome editing, but the strict requirement for an NGG protospacer-adjacent motif (PAM) sequence immediately next to the DNA target limits the number of editable genes. Recently developed Cas9 variants have been engineered with relaxed PAM requirements, including SpG-Cas9 (SpG) and the nearly PAM-less SpRY-Cas9 (SpRY). However, the molecular mechanisms of how SpRY recognizes all potential PAM sequences remains unclear. Here, we combine structural and biochemical approaches to determine how SpRY interrogates DNA and recognizes target sites. Divergent PAM sequences can be accommodated through conformational flexibility within the PAM-interacting region, which facilitates tight binding to off-target DNA sequences. Nuclease activation occurs ~1000-fold slower than for Streptococcus pyogenes Cas9, enabling us to directly visualize multiple on-pathway intermediate states. Experiments with SpG position it as an intermediate enzyme between Cas9 and SpRY. Our findings shed light on the molecular mechanisms of PAMless genome editing."}],"month":"04","type":"journal_article","file_date_updated":"2024-05-13T11:46:19Z","dataavailabilitystatement":"The structures and associated atomic coordinates have been deposited into the Electron Microscopy Data Bank (EMDB) and Protein Data Bank (PDB) with accession codes SpRY NAC PAM 20 bp (EMD-40740 and PDB 8SRS), SpRY NGG PAM (EMD-40681 and PDB 8SPQ), SpRY NTC PAM (EMD-40705 and PDB 8SQH), SpRY NAC PAM 0 bp (EMD-41073 and PDB 8T6O), SpRY NAC PAM 2 bp (EMD-41074 and PDB 8T6P), SpRY NAC PAM 3 bp (EMD-41085 and PDB 8T76), SpRY NAC PAM 10 bp (EMD-41079 and PDB 8T6S), SpRY NAC PAM 13 bp (EMD-41080 and PDB 8T6T), SpRY NAC PAM 18 bp (EMD-41083 and PDB 8T6X), SpRY off-target 1 bp (EMD-41084 and PDB 8T6Y), SpRY off-target 6* bp (EMD-41086 and PDB 8T77), SpRY off-target 8* bp (EMD-41087 and PDB 8T78), SpRY off-target 10* bp (EMD-41088 and PDB 8T79), SpRYmer (EMD-41093 and PDB 8T7S), SpG NGG PAM (EMD-41867 and PDB 8U3Y), and SpG NGC PAM (EMD-41775 and PDB 8TZZ). Source data are provided with this paper.","date_published":"2024-04-30T00:00:00Z","status":"public","publication_status":"published","supplementarymaterial":"yes","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)","image":"/images/cc_by.png"},"oa_version":"Published Version","publication_identifier":{"eissn":["2041-1723"]},"das_tickbox":"1","day":"30","has_accepted_license":"1","corr_author":"1","fulldoi":"https://doi.org/10.1038/s41467-024-47830-3","researchdata_availability":"yes","department":[{"_id":"JaBr"}],"author":[{"first_name":"Grace N.","last_name":"Hibshman","full_name":"Hibshman, Grace N."},{"full_name":"Bravo, Jack Peter Kelly","last_name":"Bravo","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e","first_name":"Jack Peter Kelly","orcid":"0000-0003-0456-0753"},{"first_name":"Matthew M.","last_name":"Hooper","full_name":"Hooper, Matthew M."},{"first_name":"Tyler L.","full_name":"Dangerfield, Tyler L.","last_name":"Dangerfield"},{"full_name":"Zhang, Hongshan","last_name":"Zhang","first_name":"Hongshan"},{"last_name":"Finkelstein","full_name":"Finkelstein, Ilya J.","first_name":"Ilya J."},{"first_name":"Kenneth A.","full_name":"Johnson, Kenneth A.","last_name":"Johnson"},{"first_name":"David W.","full_name":"Taylor, David W.","last_name":"Taylor"}],"article_type":"original","article_number":"3663","pmid":1,"external_id":{"pmid":["38688943"]},"quality_controlled":"1","acknowledgement":"We thank I. Stohkendl in the Taylor group for insightful discussions. This work was supported in part by Welch Foundation grants F-1808 (to I.J.F.), and F-1938 (to D.W.T.), the National Institutes of Health R01GM124141 (to I.J.F.), R01AI110577 (to K.A.J.), and R35GM138348 (to D.W.T.), and a Robert J. Kleberg, Jr. and Helen C. Kleberg Foundation Medical Research Grant (to D.W.T.). The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.","date_created":"2024-05-12T22:01:00Z","doi":"10.1038/s41467-024-47830-3","language":[{"iso":"eng"}],"intvolume":"        15","ddc":["570"],"scopus_import":"1","date_updated":"2026-10-02T12:00:51Z","oa":1,"title":"Unraveling the mechanisms of PAMless DNA interrogation by SpRY-Cas9","DOAJ_listed":"1","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","_id":"15372","volume":15,"citation":{"ieee":"G. N. Hibshman <i>et al.</i>, “Unraveling the mechanisms of PAMless DNA interrogation by SpRY-Cas9,” <i>Nature Communications</i>, vol. 15. Springer Nature, 2024.","mla":"Hibshman, Grace N., et al. “Unraveling the Mechanisms of PAMless DNA Interrogation by SpRY-Cas9.” <i>Nature Communications</i>, vol. 15, 3663, Springer Nature, 2024, doi:<a href=\"https://doi.org/10.1038/s41467-024-47830-3\">10.1038/s41467-024-47830-3</a>.","short":"G.N. Hibshman, J.P.K. Bravo, M.M. Hooper, T.L. Dangerfield, H. Zhang, I.J. Finkelstein, K.A. Johnson, D.W. Taylor, Nature Communications 15 (2024).","ista":"Hibshman GN, Bravo JPK, Hooper MM, Dangerfield TL, Zhang H, Finkelstein IJ, Johnson KA, Taylor DW. 2024. Unraveling the mechanisms of PAMless DNA interrogation by SpRY-Cas9. Nature Communications. 15, 3663.","apa":"Hibshman, G. N., Bravo, J. P. K., Hooper, M. M., Dangerfield, T. L., Zhang, H., Finkelstein, I. J., … Taylor, D. W. (2024). Unraveling the mechanisms of PAMless DNA interrogation by SpRY-Cas9. <i>Nature Communications</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41467-024-47830-3\">https://doi.org/10.1038/s41467-024-47830-3</a>","ama":"Hibshman GN, Bravo JPK, Hooper MM, et al. Unraveling the mechanisms of PAMless DNA interrogation by SpRY-Cas9. <i>Nature Communications</i>. 2024;15. doi:<a href=\"https://doi.org/10.1038/s41467-024-47830-3\">10.1038/s41467-024-47830-3</a>","chicago":"Hibshman, Grace N., Jack Peter Kelly Bravo, Matthew M. Hooper, Tyler L. Dangerfield, Hongshan Zhang, Ilya J. Finkelstein, Kenneth A. Johnson, and David W. Taylor. “Unraveling the Mechanisms of PAMless DNA Interrogation by SpRY-Cas9.” <i>Nature Communications</i>. Springer Nature, 2024. <a href=\"https://doi.org/10.1038/s41467-024-47830-3\">https://doi.org/10.1038/s41467-024-47830-3</a>."},"file":[{"success":1,"creator":"dernst","checksum":"509c65919067a03ef8ad65c7192cd860","access_level":"open_access","date_created":"2024-05-13T11:46:19Z","date_updated":"2024-05-13T11:46:19Z","file_name":"2024_NatureComm_Hibshman.pdf","relation":"main_file","content_type":"application/pdf","file_size":7477013,"file_id":"15386"}],"publication":"Nature Communications"},{"OA_place":"repository","corr_author":"1","fulldoi":"https://doi.org/10.1038/s41586-024-07515-9","article_type":"original","researchdata_availability":"yes","department":[{"_id":"JaBr"}],"author":[{"full_name":"Bravo, Jack Peter Kelly","last_name":"Bravo","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e","first_name":"Jack Peter Kelly","orcid":"0000-0003-0456-0753"},{"last_name":"Ramos","full_name":"Ramos, Delisa A.","first_name":"Delisa A."},{"first_name":"Rodrigo","full_name":"Fregoso Ocampo, Rodrigo","last_name":"Fregoso Ocampo"},{"last_name":"Ingram","full_name":"Ingram, Caiden","first_name":"Caiden"},{"first_name":"David W.","last_name":"Taylor","full_name":"Taylor, David W."}],"publication_identifier":{"eissn":["1476-4687"],"issn":["0028-0836"]},"supplementarymaterial":"yes","oa_version":"Submitted Version","day":"27","das_tickbox":"1","type":"journal_article","publication_status":"published","dataavailabilitystatement":"Structures of the DdmE in complex with guide and target, the DdmD monomer in complex with ssDNA, the DdmDE handover complex, the DdmD dimer and the DdmD dimer in complex with ssDNA have been deposited in the Electron Microscopy Data Bank with the accession codes EMD-41781, EMD-41790, EMD-41865, EMD-44825 and EMD-41785, respectively. Associated atomic coordinates have been deposited in the Protein Data Bank with the accession codes 8U0J, 8U0W, 8U3K, 9BVQ and 8U0U, respectively. Source data are provided with this paper.","date_published":"2024-06-27T00:00:00Z","status":"public","abstract":[{"lang":"eng","text":"Although eukaryotic Argonautes have a pivotal role in post-transcriptional gene regulation through nucleic acid cleavage, some short prokaryotic Argonaute variants (pAgos) rely on auxiliary nuclease factors for efficient foreign DNA degradation1. Here we reveal the activation pathway of the DNA defence module DdmDE system, which rapidly eliminates small, multicopy plasmids from the Vibrio cholerae seventh pandemic strain (7PET)2. Through a combination of cryo-electron microscopy, biochemistry and in vivo plasmid clearance assays, we demonstrate that DdmE is a catalytically inactive, DNA-guided, DNA-targeting pAgo with a distinctive insertion domain. We observe that the helicase-nuclease DdmD transitions from an autoinhibited, dimeric complex to a monomeric state upon loading of single-stranded DNA targets. Furthermore, the complete structure of the DdmDE–guide–target handover complex provides a comprehensive view into how DNA recognition triggers processive plasmid destruction. Our work establishes a mechanistic foundation for how pAgos utilize ancillary factors to achieve plasmid clearance, and provides insights into anti-plasmid immunity in bacteria.\r\n\r\n"}],"article_processing_charge":"No","year":"2024","publisher":"Springer Nature","month":"06","_id":"17442","volume":630,"page":"961-967","publication":"Nature","citation":{"ama":"Bravo JPK, Ramos DA, Fregoso Ocampo R, Ingram C, Taylor DW. Plasmid targeting and destruction by the DdmDE bacterial defence system. <i>Nature</i>. 2024;630(8018):961-967. doi:<a href=\"https://doi.org/10.1038/s41586-024-07515-9\">10.1038/s41586-024-07515-9</a>","chicago":"Bravo, Jack Peter Kelly, Delisa A. Ramos, Rodrigo Fregoso Ocampo, Caiden Ingram, and David W. Taylor. “Plasmid Targeting and Destruction by the DdmDE Bacterial Defence System.” <i>Nature</i>. Springer Nature, 2024. <a href=\"https://doi.org/10.1038/s41586-024-07515-9\">https://doi.org/10.1038/s41586-024-07515-9</a>.","apa":"Bravo, J. P. K., Ramos, D. A., Fregoso Ocampo, R., Ingram, C., &#38; Taylor, D. W. (2024). Plasmid targeting and destruction by the DdmDE bacterial defence system. <i>Nature</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41586-024-07515-9\">https://doi.org/10.1038/s41586-024-07515-9</a>","short":"J.P.K. Bravo, D.A. Ramos, R. Fregoso Ocampo, C. Ingram, D.W. Taylor, Nature 630 (2024) 961–967.","ista":"Bravo JPK, Ramos DA, Fregoso Ocampo R, Ingram C, Taylor DW. 2024. Plasmid targeting and destruction by the DdmDE bacterial defence system. Nature. 630(8018), 961–967.","ieee":"J. P. K. Bravo, D. A. Ramos, R. Fregoso Ocampo, C. Ingram, and D. W. Taylor, “Plasmid targeting and destruction by the DdmDE bacterial defence system,” <i>Nature</i>, vol. 630, no. 8018. Springer Nature, pp. 961–967, 2024.","mla":"Bravo, Jack Peter Kelly, et al. “Plasmid Targeting and Destruction by the DdmDE Bacterial Defence System.” <i>Nature</i>, vol. 630, no. 8018, Springer Nature, 2024, pp. 961–67, doi:<a href=\"https://doi.org/10.1038/s41586-024-07515-9\">10.1038/s41586-024-07515-9</a>."},"title":"Plasmid targeting and destruction by the DdmDE bacterial defence system","oa":1,"OA_type":"green","scopus_import":"1","date_updated":"2026-10-02T11:59:25Z","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","main_file_link":[{"open_access":"1","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC11649018/"}],"language":[{"iso":"eng"}],"doi":"10.1038/s41586-024-07515-9","intvolume":"       630","pmid":1,"external_id":{"pmid":["38740055"]},"issue":"8018","acknowledgement":"We thank K. Kiernan, G. Hibshman and I. Strohkendl for insightful discussions and comments on the manuscript, and R. Lin for assistance with the ATPase assay. Data were collected at the Sauer Structural Biology Laboratory at the University of Texas at Austin. This work was supported in part by the National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH) R35GM138348 (to D.W.T.) and Welch Foundation research grant F-1938 (to D.W.T.).","date_created":"2024-08-19T09:41:18Z","quality_controlled":"1"},{"status":"public","date_published":"2024-10-01T00:00:00Z","publication_status":"published","type":"journal_article","month":"10","publisher":"Taylor & Francis","year":"2024","article_processing_charge":"No","department":[{"_id":"JaBr"}],"author":[{"orcid":"0000-0003-0456-0753","first_name":"Jack Peter Kelly","id":"96aecfa5-8931-11ee-af30-aa6a5d6eee0e","last_name":"Bravo","full_name":"Bravo, Jack Peter Kelly"}],"researchdata_availability":"no","article_type":"letter_note","fulldoi":"https://doi.org/10.1080/17460913.2024.2389720","corr_author":"1","OA_place":"publisher","das_tickbox":"0","has_accepted_license":"1","day":"01","oa_version":"Published Version","supplementarymaterial":"no","publication_identifier":{"eissn":["1746-0921"],"issn":["1746-0913"]},"isi":1,"intvolume":"        19","ddc":["570"],"doi":"10.1080/17460913.2024.2389720","language":[{"iso":"eng"}],"quality_controlled":"1","date_created":"2024-09-05T07:32:00Z","acknowledgement":"I would like to thank K Kiernan for insightful comments and feedback. J P K Bravo is supported by IST Austria.","issue":"15","external_id":{"isi":["001306115400001"],"pmid":["39230568"]},"pmid":1,"citation":{"chicago":"Bravo, Jack Peter Kelly. “Anti-Plasmid Immunity: A Key to Pathogen Success?” <i>Future Microbiology</i>. Taylor &#38; Francis, 2024. <a href=\"https://doi.org/10.1080/17460913.2024.2389720\">https://doi.org/10.1080/17460913.2024.2389720</a>.","ama":"Bravo JPK. Anti-plasmid immunity: A key to pathogen success? <i>Future Microbiology</i>. 2024;19(15):1269-1272. doi:<a href=\"https://doi.org/10.1080/17460913.2024.2389720\">10.1080/17460913.2024.2389720</a>","apa":"Bravo, J. P. K. (2024). Anti-plasmid immunity: A key to pathogen success? <i>Future Microbiology</i>. Taylor &#38; Francis. <a href=\"https://doi.org/10.1080/17460913.2024.2389720\">https://doi.org/10.1080/17460913.2024.2389720</a>","ista":"Bravo JPK. 2024. Anti-plasmid immunity: A key to pathogen success? Future Microbiology. 19(15), 1269–1272.","short":"J.P.K. Bravo, Future Microbiology 19 (2024) 1269–1272.","mla":"Bravo, Jack Peter Kelly. “Anti-Plasmid Immunity: A Key to Pathogen Success?” <i>Future Microbiology</i>, vol. 19, no. 15, Taylor &#38; Francis, 2024, pp. 1269–72, doi:<a href=\"https://doi.org/10.1080/17460913.2024.2389720\">10.1080/17460913.2024.2389720</a>.","ieee":"J. P. K. Bravo, “Anti-plasmid immunity: A key to pathogen success?,” <i>Future Microbiology</i>, vol. 19, no. 15. Taylor &#38; Francis, pp. 1269–1272, 2024."},"publication":"Future Microbiology","page":"1269-1272","volume":19,"_id":"17494","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1080/17460913.2024.2389720"}],"user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","date_updated":"2026-10-02T12:01:31Z","scopus_import":"1","OA_type":"free access","oa":1,"title":"Anti-plasmid immunity: A key to pathogen success?"}]