Structural basis for plasmid restriction by SMC JET nuclease
Open accessPublished version of a preprint
Abstract
DNA loop-extruding SMC complexes play crucial roles in chromosome folding and DNA immunity. Prokaryotic SMC Wadjet (JET) complexes limit the spread of plasmids through DNA cleavage, yet the mechanisms for plasmid recognition are unresolved. We show that artificial DNA circularization renders linear DNA susceptible to JET nuclease cleavage. Unlike free DNA, JET cleaves immobilized plasmid DNA at a specific site, the plasmid-anchoring point, showing that the anchor hinders DNA extrusion but not DNA cleavage. Structures of plasmid-bound JetABC reveal two presumably stalled SMC motor units that are drastically rearranged from the resting state, together entrapping a U-shaped DNA segment, which is further converted to kinked V-shaped cleavage substrate by JetD nuclease binding. Our findings uncover mechanical bending of residual unextruded DNA as molecular signature for plasmid recognition and non-self DNA elimination. We moreover elucidate key elements of SMC loop extrusion, including the motor direction and the structure of a DNA-holding state.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,260 · see citing works
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. D. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 27,510 · see citing works
ColabFold - Making protein folding accessible to all
Mirdita, M., Schütze, K., Moriwaki, Y., Heo, L., Ovchinnikov, S., & Steinegger, M. (2021) · doi:10.1101/2021.08.15.456425 · Cited by 9,391 · see citing works
UCSF ChimeraX : Structure visualization for researchers, educators, and developers
Pettersen, E. F., Goddard, T. D., Huang, C. C., Meng, E. C., Couch, G. S., Croll, T. I., Morris, J. H., & Ferrin, T. E. (2020) · Protein Science · doi:10.1002/pro.3943 · Cited by 9,327 · see citing works
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 9,168 · see citing works
Liebschner, D. C., Afonine, P. V., Baker, M. L., Bunkòczi, G., Chen, V. B., Croll, T. I., Hintze, B. J., Hung, L., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 6,709 · see citing works
UCSF ChimeraX: Meeting modern challenges in visualization and analysis
Goddard, T. D., Huang, C. C., Meng, E. C., Pettersen, E. F., Couch, G. S., Morris, J. H., & Ferrin, T. E. (2018) · Protein Science · doi:10.1002/pro.3235 · Cited by 5,267 · see citing works
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
Davis, I., Leaver‐Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., Snoeyink, J. S., Richardson, J. S., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm216 · Cited by 3,915 · see citing works
Protein complex prediction with AlphaFold-Multimer
Evans, R., O’Neill, M., Pritzel, A., Antropova, N., Senior, A., Green, T., Žídek, A., Bates, R., Blackwell, S., Yim, J., et al. (2021) · doi:10.1101/2021.10.04.463034 · Cited by 3,808 · see citing works
Croll, T. (2018) · Acta Crystallographica Section D: Structural Biology · doi:10.1107/s2059798318002425 · Cited by 1,934 · see citing works
Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction
Punjani, A., Zhang, H., & Fleet, D. J. (2020) · Nature Methods · doi:10.1038/s41592-020-00990-8 · Cited by 1,559 · see citing works
Structural Origins of High-Affinity Biotin Binding to Streptavidin
Weber, P. C., Ohlendorf, D. H., Wendoloski, J. J., & Salemme, F. R. (1989) · Science · doi:10.1126/science.2911722 · Cited by 1,224 · see citing works
Systematic discovery of antiphage defense systems in the microbial pangenome
Doron, S., Melamed, S., Ofir, G., Leavitt, A., Lopatina, A., Keren, M., Amitai, G., & Sorek, R. (2018) · Science · doi:10.1126/science.aar4120 · Cited by 1,190 · see citing works
Punjani, A., & Fleet, D. J. (2021) · Journal of Structural Biology · doi:10.1016/j.jsb.2021.107702 · Cited by 928 · see citing works
Addressing Preferred Specimen Orientation in Single-Particle Cryo-EM through Tilting
Tan, Y.-Z., Baldwin, P. R., Davis, J., Williamson, J., Potter, C., Carragher, B., & Lyumkis, D. (2017) · Nature Methods · doi:10.1038/nmeth.4347 · Cited by 920 · see citing works
DNA loop extrusion by human cohesin
Davidson, I. F., Bauer, B., Goetz, D., Tang, W., Wutz, G., & Peters, J.-M. (2019) · Science · doi:10.1126/science.aaz3418 · Cited by 863 · see citing works
Casañal, A., Lohkamp, B., & Emsley, P. (2019) · Protein Science · doi:10.1002/pro.3791 · Cited by 812 · see citing works
Real-time imaging of DNA loop extrusion by condensin
Ganji, M., Shaltiel, I. A., Bisht, S., Kim, E., Kalichava, A., Haering, C. H., & Dekker, C. (2018) · Science · doi:10.1126/science.aar7831 · Cited by 793 · see citing works
New tools for the analysis and validation of cryo-EM maps and atomic models
Afonine, P. V., Klaholz, B. P., Moriarty, N. W., Poon, B. K., Sobolev, O. V., Terwilliger, T. C., Adams, P. D., & Urzhumtsev, A. (2018) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798318009324 · Cited by 719 · see citing works
Human cohesin compacts DNA by loop extrusion
Kim, Y., Shi, Z., Zhang, H., Finkelstein, I. J., & Yu, H. (2019) · Science · doi:10.1126/science.aaz4475 · Cited by 701 · see citing works
RecBCD Enzyme and the Repair of Double-Stranded DNA Breaks
Dillingham, M. S., & Kowalczykowski, S. C. (2008) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00020-08 · Cited by 586 · see citing works
Genome folding through loop extrusion by SMC complexes
Davidson, I. F., & Peters, J. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00349-7 · Cited by 507 · see citing works
Sae2 promotes dsDNA endonuclease activity within Mre11–Rad50–Xrs2 to resect DNA breaks
Cannavò, E., & Ćejka, P. (2014) · Nature · doi:10.1038/nature13771 · Cited by 428 · see citing works
Measurement of atom resolvability in cryo-EM maps with Q-scores
Pintilie, G. D., Zhang, K., Su, Z., Li, S., Schmid, M. F., & Chiu, W. (2020) · Nature Methods · doi:10.1038/s41592-020-0731-1 · Cited by 404 · see citing works
Bao, Y., Lies, D. P., Fu, H., & Roberts, G. P. (1991) · Gene · doi:10.1016/0378-1119(91)90604-a · Cited by 338 · see citing works
Organization of Chromosomal DNA by SMC Complexes
Yatskevich, S., Rhodes, J., & Nasmyth, K. (2019) · Annual Review of Genetics · doi:10.1146/annurev-genet-112618-043633 · Cited by 337 · see citing works
Structural basis for gate-DNA recognition and bending by type IIA topoisomerases
Dong, K. C., & Berger, J. M. (2007) · Nature · doi:10.1038/nature06396 · Cited by 316 · see citing works
Wang, X., Brandão, H. B., Le, T. B. K., Laub, M. T., & Rudner, D. Z. (2017) · Science · doi:10.1126/science.aai8982 · Cited by 293 · see citing works
The Bloom's Syndrome Helicase Can Promote the Regression of a Model Replication Fork
Ralf, C., Hickson, I. D., & Wu, L. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604268200 · Cited by 222 · see citing works
Cryo-EM structure of the human cohesin-NIPBL-DNA complex
Shi, Z.-B., Gao, H.-S., Bai, X.-C., & Yu, H.-T. (2020) · Science · doi:10.1126/science.abb0981 · Cited by 196 · see citing works
Stark, W. M., Sherratt, D. J., & Boocock, M. R. (1989) · Cell · doi:10.1016/0092-8674(89)90111-6 · Cited by 194 · see citing works
Towards a unified Model of SMC Complex Function
Hassler, M., Shaltiel, I. A., & Haering, C. (2018) · Current Biology · doi:10.1016/j.cub.2018.08.034 · Cited by 162 · see citing works
Structure of Full-Length SMC and Rearrangements Required for Chromosome Organization
Diebold-Durand, M.-L., Lee, H., Ruiz-Ávila, L. B., Noh, H., Shin, H.-C., Im, H., Bock, F., Burmann, F., Durand, A., Basfeld, A., et al. (2017) · Molecules and Cells · doi:10.1016/j.molcel.2017.06.010 · Cited by 155 · see citing works
Self-citationWoo, J.-S., Lim, J.-H., Shin, H.-C., Suh, M., Ku, B., Lee, K.-H., Joo, K., Robinson, H., Lee, J., Park, S.-Y., et al. (2009) · Cell · doi:10.1016/j.cell.2008.10.050 · Cited by 147 · see citing works
A Structure-Based Mechanism for DNA Entry into the Cohesin Ring
Higashi, T. L., Eickhoff, P., Sousa, J. S., Locke, J., Nans, A., Flynn, H. R., Snijders, A. P., Papageorgiou, G., O’Reilly, N., Chen, Z. A., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.07.013 · Cited by 146 · see citing works
Reginato, G., Cannavò, E., & Ćejka, P. (2017) · Genes & Development · doi:10.1101/gad.308254.117 · Cited by 138 · see citing works
The Smc5/6 complex is a DNA loop-extruding motor
Pradhan, B., Kanno, T., Igarashi, M. U., Loke, M. S., Baaske, M. D., Wong, J. S. K., Jeppsson, K. E., Björkegren, C., & Kim, E. (2023) · Nature · doi:10.1038/s41586-023-05963-3 · Cited by 136 · see citing works
Mechanism of DNA End Sensing and Processing by the Mre11-Rad50 Complex
Käshammer, L., Saathoff, J.-H., Lammens, K., Gut, F., Bartho, J. D., Alt, A., Keßler, B., & Hopfner, K. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.035 · Cited by 131 · see citing works
SMC Complexes Can Traverse Physical Roadblocks Bigger Than Their Ring Size
Pradhan, B., Barth, R., Kim, E., Davidson, I. F., Bauer, B. W., van Laar, T., Yang, W., Ryu, J., van der Torre, J., Peters, J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111491 · Cited by 131 · see citing works
An asymmetric SMC–kleisin bridge in prokaryotic condensin
Bürmann, F., Shin, H., Basquin, J., Soh, Y., Giménez-Oya, V., Kim, Y., Oh, B., & Gruber, S. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2488 · Cited by 121 · see citing works
Self-citationPlasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstaclesPreprint
Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., & Sung, P. (2017) · Genes & Development · doi:10.1101/gad.307900.117 · Cited by 117 · see citing works
Marko, J., Rios, P. D. L., Barducci, A., & Gruber, S. (2018) · bioRxiv · doi:10.1093/nar/gkz497 · Cited by 116 · see citing works
Self-citationCTCF and R-loops are boundaries of cohesin-mediated DNA looping
Zhang, H., Shi, Z., Banigan, E. J., Kim, Y., Yu, H., Bai, X., & Finkelstein, I. J. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.07.006 · Cited by 116 · see citing works
A hold-and-feed mechanism drives directional DNA loop extrusion by condensin
Shaltiel, I. A., Datta, S., Lecomte, L., Hassler, M., Kschonsak, M., Bravo, S., Stober, C., Ormanns, J., Eustermann, S., & Haering, C. H. (2022) · Science · doi:10.1126/science.abm4012 · Cited by 112 · see citing works
Deep, A., Gu, Y., Gao, Y.-Q., Ego, K. M., Herzik, M. A., Zhou, H., & Corbett, K. D. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.008 · Cited by 106 · see citing works
Holoenzyme assembly and ATP-mediated conformational dynamics of topoisomerase VI
Corbett, K. D., Benedetti, P., & Berger, J. M. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1264 · Cited by 104 · see citing works
The MRE11 complex: A versatile toolkit for the repair of broken DNA
Reginato, G., & Ćejka, P. (2020) · DNA repair · doi:10.1016/j.dnarep.2020.102869 · Cited by 95 · see citing works
Structural and functional characterization of the Spo11 core complex
Claeys Bouuaert, C., Tischfield, S. E., Pu, S., Mimitou, E. P., Arias-Palomo, E., Berger, J. M., & Keeney, S. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00534-w · Cited by 87 · see citing works
Role of the Mre11 Complex in Preserving Genome Integrity
Oh, J., & Symington, L. S. (2018) · Genes · doi:10.3390/genes9120589 · Cited by 85 · see citing works
A new family of bacterial condensins
Petrushenko, Z. M., She, W., & Rybenkov, V. V. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07763.x · Cited by 83 · see citing works
Böhm, K., Giacomelli, G., Schmidt, A., Imhof, A., Koszul, R., Marbouty, M., & Bramkamp, M. (2019) · Nature Communications · doi:10.1038/s41467-020-15238-4 · Cited by 75 · see citing works
Cryo-EM structure of MukBEF reveals DNA loop entrapment at chromosomal unloading sites
Bürmann, F., Funke, L. F. H., Chin, J. W., & Löwe, J. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.10.011 · Cited by 74 · see citing works
The MukF subunit of Escherichia coli condensin: architecture and functional relationship to kleisins
Fennell-Fezzie, R., Gradia, S., Akey, D. L., & Berger, J. M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600680 · Cited by 70 · see citing works
Panas, M. W., Jain, P., Yang, H., Mitra, S., Biswas, D., Wattam, A. R., Letvin, N. L., & Jacobs, W. R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414207111 · Cited by 62 · see citing works
Transient DNA Occupancy of the SMC Interarm Space in Prokaryotic Condensin
Nunez, R. J. V., Avila, L. B. R., & Gruber, S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.05.001 · Cited by 61 · see citing works
Self-citationDNA-measuring Wadjet SMC ATPases restrict smaller circular plasmids by DNA cleavage
Liu, H. W., Roisné-Hamelin, F., Beckert, B., Li, Y., Myasnikov, A., & Gruber, S. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.11.015 · Cited by 53 · see citing works
Self-citationDNA segment capture by Smc5/6 holocomplexes
Taschner, M., & Gruber, S. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-00956-2 · Cited by 39 · see citing works
Self-citationNicking enzyme–based internal labeling of DNA at multiple loci
Luzzietti, N., Knappe, S., Richter, I., & Seidel, R. (2012) · Nature Protocols · doi:10.1038/nprot.2012.008 · Cited by 39 · see citing works
The MksG nuclease is the executing part of the bacterial plasmid defense system MksBEFG
Weiß, M., Giacomelli, G., Assaya, M. B., Grundt, F., Haouz, A., Peng, F., Petrella, S., Wehenkel, A. M., & Bramkamp, M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad130 · Cited by 37 · see citing works
Structural mechanism of endonucleolytic processing of blocked DNA ends and hairpins by Mre11-Rad50
Gut, F., Käshammer, L., Lammens, K., Bartho, J. D., Boggusch, A.-M., van de Logt, E., Keßler, B., & Hopfner, K. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.07.019 · Cited by 34 · see citing works
Condensin-Mediated Chromosome Folding and Internal Telomeres Drive Dicentric Severing by Cytokinesis
Guérin, T. M., Béneut, C., Barinova, N., López, V., Lazar‐Stefanita, L., Deshayes, A., Thierry, A., Koszul, R., Dubrana, K., & Marcand, S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.05.021 · Cited by 32 · see citing works
SMC-based immunity against extrachromosomal DNA elements
Liu, H. W., Roisné-Hamelin, F., & Gruber, S. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221395 · Cited by 31 · see citing works
Self-citationSMC complexes sweeping through the chromosome: going with the flow and against the tide
Gruber, S. (2018) · Current Opinion in Microbiology · doi:10.1016/j.mib.2017.10.004 · Cited by 30 · see citing works
Self-citationStructural biology of SMC complexes across the tree of life
Burmann, F., & Löwe, J. (2023) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2023.102598 · Cited by 29 · see citing works
Hopfner, K. (2023) · Biochemical Society Transactions · doi:10.1042/bst20220754 · Cited by 27 · see citing works
The SMC5/6 complex: An emerging antiviral restriction factor that can silence episomal DNA
Irwan, I. D., & Cullen, B. R. (2023) · PLoS Pathogens · doi:10.1371/journal.ppat.1011180 · Cited by 25 · see citing works
Adaptive Cartesian and torsional restraints for interactive model rebuilding
Croll, T. I., & Read, R. J. (2021) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798321001145 · Cited by 24 · see citing works
Cryo-EM structures of the Spo11 core complex bound to DNA
Yu, Y., Wang, J., Liu, K., Zheng, Z., Arter, M., Claeys Bouuaert, C., Pu, S., Patel, D. J., & Keeney, S. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01382-8 · Cited by 20 · see citing works
A low Smc flux avoids collisions and facilitates chromosome organization in Bacillus subtilis
Anchimiuk, A., Lioy, V., Bock, F., Minnen, A., Boccard, F., & Gruber, S. (2021) · eLife · doi:10.7554/elife.65467 · Cited by 19 · see citing works
Self-citationMeng, B., Lan, K., Xie, J., Lerner, R. A., Wilson, I. A., & Yang, B. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1918844117 · Cited by 17 · see citing works
Telomere protein arrays stall DNA loop extrusion by condensinPreprint
Analikwu, B. T., Deshayes, A., van der Torre, J., Guérin, T. M., Katan, A., Béneut, C., Barth, R., Phipps, J., Scolari, V., Veaute, X., et al. (2023) · bioRxiv · doi:10.1101/2023.10.29.564563 · Cited by 10 · see citing works
Diagouraga, B., Tambones, I., Carivenc, C., Bechara, C., Nadal, M., de Massy, B., le Maire, A., & Robert, T. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae587 · Cited by 10 · see citing works
Flagged first, then by citations
1 of the 74 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
A unified model for cohesin function in sister chromatid cohesion and chromatin loop formation
Uhlmann, F. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.02.005 · Cited by 44 · see citing works
An extrinsic motor directs chromatin loop formation by cohesin
Guérin, T. M., Barrington, C., Pobegalov, G., Molodtsov, M. I., & Uhlmann, F. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00202-5 · Cited by 43 · see citing works
The extended mobility of plasmids
Garcillán-Barcia, M. P., de la Cruz, F., & Rocha, E. P. C. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf652 · Cited by 39 · see citing works
Loop-extrusion-mediated plasmid DNA cleavage by the bacterial SMC Wadjet complex
Pradhan, B., Deep, A., König, J., Baaske, M. D., Corbett, K. D., & Kim, E. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.11.002 · Cited by 35 · see citing works
Structural basis of the RNA-mediated Retron-Eco2 oligomerization
Wang, Y., Wang, C., Yin, Y., Cui, Y., Dai, Z., Liu, C., Chen, Y., Guan, Z., & Zou, T. (2025) · Cell Discovery · doi:10.1038/s41421-025-00823-y · Cited by 14 · see citing works
Structural basis of antiphage defence by an ATPase-associated reverse transcriptase
George, J. T., Burman, N., Wilkinson, R. A., de Silva, S., McKelvey-Pham, Q., Buyukyoruk, M., Dale, A., Landman, H., Graham, A. B., DeLuca, S. Z., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-63285-6 · Cited by 14 · see citing works
Structure and activation mechanism of a Lamassu phage and plasmid defense system
Li, Y., Adams, D. W., Liu, H. W., Shaw, S. J., Uchikawa, E., Jaskólska, M., Stutzmann, S., Righi, L., Szczelkun, M. D., Blokesch, M., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01677-4 · Cited by 14 · see citing works
Self-citationNucleic acid recognition during prokaryotic immunity
Baca, C. F., & Marraffini, L. A. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.12.007 · Cited by 13 · see citing works
Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic
Bürmann, F., Clifton, B., Koekemoer, S., Wilkinson, O. J., Kimanius, D., Dillingham, M. S., & Löwe, J. (2025) · Cell · doi:10.1016/j.cell.2025.02.032 · Cited by 12 · see citing works
Qi, S., Shi, Z., & Yu, H. (2025) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2025.102310 · Cited by 11 · see citing works
The SMC Hinge is a Selective Gate for Obstacle Bypass
Liu, H. W., Roisné-Hamelin, F., Taschner, M., Collier, J., Srinivasan, M., & Gruber, S. (2025) · Nature Communications · doi:10.1038/s41467-025-65408-5 · Cited by 11 · see citing works
Self-citationIn vitro dynamics of DNA loop extrusion by structural maintenance of chromosomes complexes
Rutkauskas, M., & Kim, E. (2024) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2024.102284 · Cited by 6 · see citing works
Nucleotide signals coordinate activation and inhibition of bacterial immunity
Yamaguchi, S., Fernandez, S. G., Wassarman, D. R., Lüders, M., Schwede, F., & Kranzusch, P. J. (2026) · Nature · doi:10.1038/s41586-026-10135-0 · Cited by 6 · see citing works
Bacterial WYL domain transcriptional repressors sense single-stranded DNA to control gene expression
Blankenchip, C. L., & Corbett, K. D. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1101 · Cited by 6 · see citing works
4G cloning: rapid gene assembly for expression of multisubunit protein complexes in diverse hosts
Taschner, M., Dickinson, J. B., Roisné-Hamelin, F., & Gruber, S. (2024) · Life Science Alliance · doi:10.26508/lsa.202402899 · Cited by 5 · see citing works
Self-citationStructure of a type II SMC Wadjet complex from Neobacillus vireti
(2025) · doi:10.1016/j.str.2025.06.004 · Cited by 4 · see citing works
Self-citationPacheco-Acosta, S., Castro-Toro, G., Rojas-Villalobos, C., Valenzuela, C., Haristoy, J. J., Zapata-Araya, A., Moya-Beltrán, A., Sepúlveda-Rebolledo, P., Pérez‐Rueda, E., Ulloa, R. J., et al. (2025) · Frontiers in Microbiology · doi:10.3389/fmicb.2025.1610279 · Cited by 4 · see citing works
Supercoiled DNA recognition and cleavage control in topoisomerase VI
Richman, D. E., Wendorff, T. J., Rashid, F., Beck, C., Yan, Q., Johnson, H. R., Eckerty, R. A., Fogg, J. M., Baker, M. L., Zechiedrich, L., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-69491-0 · Cited by 5 · see citing works
Structural Maintenance of Chromosomes Complexes
Jeppsson, K. E. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-4136-1_2 · Cited by 4 · see citing works
Submolecular video-imaging of the Smc5/6 complex topologically bound to DNA
Umeda, K., Kurokawa, Y., Kodera, N., & Murayama, Y. (2026) · Nature Communications · doi:10.1038/s41467-026-77122-x · Cited by 2 · see citing works
Phage-encoded TelN inhibits bacterial Mre11-Rad50 nuclease to protect hairpin telomeres
Houmel, M., Pellaton, N., Anchimiuk, A., & Gruber, S. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00593-z · Cited by 2 · see citing works
Self-citationMechanism of DNA entrapment by a loop-extruding Wadjet SMC motor
Roisné-Hamelin, F., Liu, H. W., Marechal, N., Uchikawa, E., Durand, A., & Gruber, S. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.09.015 · Cited by 2 · see citing works
Self-citationSMC-like Wadjet system prevents plasmid transfer into Clostridium cellulovorans
Schöllkopf, A. I., Ehrenreich, A., & Liebl, W. (2025) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-025-13551-w · Cited by 1 · see citing works
Wadjet—Keeping a watchful eye on circular DNA
Corbett, K. D., & Deep, A. (2025) · Structure · doi:10.1016/j.str.2025.08.006 · Cited by 1 · see citing works
DNA Bioconjugation with Polymer Beads Using SNAP-tag® Technology
Liu, H. W., & Gruber, S. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-5005-9_6 · Cited by 1 · see citing works
Self-citationGenomic landscape of antiviral defense systems in prokaryotes and phagesPreprint
Li, J., Gu, J., Xia, R., & Li, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.26.620412 · Cited by 1 · see citing works
Plot twists and cutting corners with atypical SMCs
Haarhuis, J. H. I., & Rowland, B. D. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.02.014
The Meeting Report on the Fifth International Conference of the Chromosomal SMC Complexes
Niki, H., & Murayama, Y. (2025) · Genes to Cells · doi:10.1111/gtc.70039
Wang, C., Duan, A.-F., Pan, D.-M., Zhao, Y.-O., Yang, J., & Sun, Y.-C. (2025) · BMC Microbiology · doi:10.1186/s12866-025-04214-x
Structural Maintenance of Chromosomes Complexes in Bacteria
Sanath-Kumar, R., Liao, Q., Ren, Z., & Wang, X. (2026) · Annual Review of Microbiology · doi:10.1146/annurev-micro-041222-034556
Himpich, S., Gaudin, T., Grass, L. M., Li, H., Loi, V. V., Chen, C., Klauck, E., Popp, P. F., Feussner, M., Kuropka, B., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118021
- Authors
- Roisné-Hamelin, F., Liu, H. W., Taschner, M., Li, Y., & Gruber, S.
- Affiliations
- University of Lausanne (CH)
- Corresponding author
- Gruber, Stephan
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2024-03
- Volume
- 84
- Issue
- 5
- Pages
- 883-896.e7
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W4391486282
- Cited by
- 34
- References
- 74
- Citations by year
- 2026: 6 · 2025: 20 · 2024: 8
- FWCI
- 9.06
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- IRIS (submittedVersion)
- SERVAL (Université de Lausanne) (submittedVersion)
- Funders
- European Research Council (724482)
- European Molecular Biology Organization (ATLF 302-2022, ALTF 490-2021, E248A)
- Université de Genève
- École Polytechnique Fédérale de Lausanne
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- loop extrusion, DNA circularization, DNA kinking, DNA bending, chromosome folding
- MeSH terms
- DNA, Endonucleases, Plasmids, Prokaryotic Cells, Cell Cycle Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review