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Repeated duplications and losses shaped SMC complex evolution from archaeal ancestors to modern eukaryotes
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Abstract
Across life, structural maintenance of chromosomes (SMC) complexes organize chromosomes. While most prokaryotes have one, eukaryotes usually possess four (condensin I, condensin II, cohesin, and SMC5/6), shaping their considerably larger genomes. Although essential, SMC complexes differ among model eukaryotes, suggesting underexplored diversity. Here, we reconstruct eukaryotic SMC complex evolution, revealing that the last eukaryotic common ancestor (LECA) had all four complexes, supporting a sophisticated LECA. Subsequently, condensin II was lost at least 30 times, making it one of the most frequently lost eukaryotic machineries. Moreover, multiple SMC complex components are more ancient and widespread than previously appreciated. Tracing prokaryotic origins, we propose that the SMC complex was already duplicated in the Thaumarchaeota-Aigarchaeota-Crenarchaeota-Korarchaeota (TACK) and Asgard archaeal ancestor, suggesting sophisticated chromosome organization in eukaryotes' archaeal ancestor. Gene duplications further expanded the eukaryotic SMC complex inventory, highlighting their significance in establishing eukaryotic complexity. Altogether, our work suggests major shifts in genome organization throughout eukaryote history.
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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
Manni, M., Berkeley, M. R., Seppey, M., Simão, F. A., & Zdobnov, E. M. (2021) · Molecular Biology and Evolution · doi:10.1093/molbev/msab199 · Cited by 6,187
Potter, S. C., Luciani, A., Eddy, S. R., Park, Y., Lopez, R., & Finn, R. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky448 · Cited by 2,607
Fast and accurate protein structure search with Foldseek
van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2022) · doi:10.1101/2022.02.07.479398 · Cited by 2,598
Fast and accurate protein structure search with Foldseek
van Kempen, M., Kim, S. S., Tumescheit, C., Mirdita, M., Lee, J., Gilchrist, C. L. M., Söding, J., & Steinegger, M. (2024) · Nature Biotechnology · doi:10.1038/s41587-023-01773-0 · Cited by 2,596
Complex archaea that bridge the gap between prokaryotes and eukaryotes
Spang, A., Saw, J. H., Jørgensen, S. L., Zaremba-Niedzwiedzka, K., Martijn, J., Lind, A. E., van Eijk, R., Schleper, C., Guy, L., & Ettema, T. J. G. (2015) · Nature · doi:10.1038/nature14447 · Cited by 1,324
Asgard archaea illuminate the origin of eukaryotic cellular complexity
Zaremba-Niedzwiedzka, K., Caceres, E. F., Saw, J. H., Bäckström, D., Juzokaite, L., Vancaester, E., Seitz, K. W., Anantharaman, K., Starnawski, P., Kjeldsen, K. U., et al. (2017) · Nature · doi:10.1038/nature21031 · Cited by 1,226
How significant is a protein structure similarity with TM-score = 0.5?
Xu, J., & Zhang, Y. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq066 · Cited by 1,142
Condensin-based chromosome organization from bacteria to vertebrates
Hirano, T. (2016) · Cell · doi:10.1016/j.cell.2016.01.033 · Cited by 389
Flagged first, then by citations
Research works printed but not linked: 108
- Szabo, 2019, Principles of genome folding into topologically associating domains, Sci. Adv., 5, 10.1126/sciadv.aaw1668 · DOI
- Davidson, 2021, Genome folding through loop extrusion by SMC complexes, Nat. Rev. Mol. Cell Biol., 22, 445, 10.1038/s41580-021-00349-7 · DOI
- Hassler, 2018, Towards a Unified Model of SMC Complex Function, Curr. Biol., 28, R1266, 10.1016/j.cub.2018.08.034 · DOI
- Makrantoni, 2018, Cohesin and chromosome segregation, Curr. Biol., 28, R688, 10.1016/j.cub.2018.05.019 · DOI
- Wells, 2017, Evolution of condensin and cohesin complexes driven by replacement of Kite by Hawk proteins, Curr. Biol., 27, R17, 10.1016/j.cub.2016.11.050 · DOI
- Bauer, 2012, Condensin II promotes the formation of chromosome territories by inducing axial compaction of polyploid interphase chromosomes, PLoS Genet., 8, 10.1371/journal.pgen.1002873 · DOI
- Jin, 2000, Centromere clustering is a major determinant of yeast interphase nuclear organization, J. Cell Sci., 113, 1903, 10.1242/jcs.113.11.1903 · DOI
- Peng, 2023, The multi-functional Smc5/6 complex in genome protection and disease, Nat. Struct. Mol. Biol., 30, 724, 10.1038/s41594-023-01015-6 · DOI
- Yoshinaga, 2021, Ubiquity and Origins of Structural Maintenance of Chromosomes (SMC) Proteins in Eukaryotes, Genome Biol. Evol., 13, 10.1093/gbe/evab256 · DOI
- King, 2019, Recurrent Losses and Rapid Evolution of the Condensin II Complex in Insects, Mol. Biol. Evol., 36, 2195, 10.1093/molbev/msz140 · DOI
- Hoencamp, 2021, 3D genomics across the tree of life reveals condensin II as a determinant of architecture type, Sci. Technol. Humanit., 372, 984
- Eme, 2023, Inference and reconstruction of the heimdallarchaeial ancestry of eukaryotes, Nature, 618, 992, 10.1038/s41586-023-06186-2 · DOI
- Prokopchuk, 2023, Lessons from the deep: mechanisms behind diversification of eukaryotic protein complexes, Biol. Rev. Camb. Philos. Soc., 98, 1910, 10.1111/brv.12988 · DOI
- O’Malley, 2016, Losing Complexity: The Role of Simplification in Macroevolution, Trends Ecol. Evol., 31, 608, 10.1016/j.tree.2016.04.004 · DOI
- Marron, 2016, The evolution of silicon transport in eukaryotes, Mol. Biol. Evol., 33, 3226, 10.1093/molbev/msw209 · DOI
- Russell, 2006, An early evolutionary origin for the minor spliceosome, Nature, 443, 863, 10.1038/nature05228 · DOI
- Tromer, 2019, Mosaic origin of the eukaryotic kinetochore, Proc. Natl. Acad. Sci. USA, 116, 12873, 10.1073/pnas.1821945116 · DOI
- Eliáš, 2016, A paneukaryotic genomic analysis of the small GTPase RABL2 underscores the significance of recurrent gene loss in eukaryote evolution, Biol. Direct, 11, 5, 10.1186/s13062-016-0107-8 · DOI
- Stairs, 2021, Anaeramoebae are a divergent lineage of eukaryotes that shed light on the transition from anaerobic mitochondria to hydrogenosomes, Curr. Biol., 31, 5605, 10.1016/j.cub.2021.10.010 · DOI
- Hirano, 2012, Condensins: universal organizers of chromosomes with diverse functions, Genes Dev., 26, 1659, 10.1101/gad.194746.112 · DOI
- Howard-Till, 2018, Condensins promote chromosome individualization and segregation during mitosis, meiosis, and amitosis in Tetrahymena thermophila, Mol. Biol. Cell, 29, 466, 10.1091/mbc.E17-07-0451 · DOI
- Howard-Till, 2019, A specialized condensin complex participates in somatic nuclear maturation in Tetrahymena thermophila, Mol. Biol. Cell, 30, 1326, 10.1091/mbc.E18-08-0487 · DOI
- Fernandes, 2019, A multigene timescale and diversification dynamics of Ciliophora evolution, Mol. Phylogenet. Evol., 139, 10.1016/j.ympev.2019.106521 · DOI
- Räschle, 2015, Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links, Sci. Technol. Humanit., 348
- Diaz, 2018, Scaffolding for Repair: Understanding Molecular Functions of the SMC5/6 Complex, Genes, 9, 10.3390/genes9010036 · DOI
- Adamus, 2020, Molecular Insights into the Architecture of the Human SMC5/6 Complex, J. Mol. Biol., 432, 3820, 10.1016/j.jmb.2020.04.024 · DOI
- Patil, 2015, Identification of the meiotic toolkit in diatoms and exploration of meiosis-specific SPO11 and RAD51 homologs in the sexual species Pseudo-nitzschia multistriata and Seminavis robusta, BMC Genom., 16, 930, 10.1186/s12864-015-1983-5 · DOI
- Alonso-Gil, 2023, NIPBL and cohesin: new take on a classic tale, Trends Cell Biol., 33, 860, 10.1016/j.tcb.2023.03.006 · DOI
- Petela, 2018, Scc2 Is a Potent Activator of Cohesin’s ATPase that Promotes Loading by Binding Scc1 without Pds5, Mol. Cell, 70, 1134, 10.1016/j.molcel.2018.05.022 · DOI
- Eme, 2011, The phylogenomic analysis of the anaphase promoting complex and its targets points to complex and modern-like control of the cell cycle in the last common ancestor of eukaryotes, BMC Evol. Biol., 11, 265, 10.1186/1471-2148-11-265 · DOI
- Prusén Mota, 2024, Sororin is an evolutionary conserved antagonist of WAPL, Nat. Commun., 15, 4729, 10.1038/s41467-024-49178-0 · DOI
- Bürmann, 2025, Mechanism of DNA capture by the MukBEF SMC complex and its inhibition by a viral DNA mimic, Cell, 188, 2465, 10.1016/j.cell.2025.02.032 · DOI · Paper page
- Minh, 2020, IQ-TREE 2: New Models and Efficient Methods for Phylogenetic Inference in the Genomic Era, Mol. Biol. Evol., 37, 1530, 10.1093/molbev/msaa015 · DOI · Paper page
- Hoang, 2018, UFBoot2: Improving the Ultrafast Bootstrap Approximation, Mol. Biol. Evol., 35, 518, 10.1093/molbev/msx281 · DOI · Paper page
- Palecek, 2015, Kite Proteins: a Superfamily of SMC/Kleisin Partners Conserved Across Bacteria, Archaea, and Eukaryotes, Structure, 23, 2183, 10.1016/j.str.2015.10.004 · DOI
- Aouad, 2022, A divide-and-conquer phylogenomic approach based on character supermatrices resolves early steps in the evolution of the Archaea, BMC Ecol. Evol., 22, 1, 10.1186/s12862-021-01952-0 · DOI
- Ouyang, 2013, Structure of the human cohesin inhibitor Wapl, Proc. Natl. Acad. Sci. USA, 110, 11355, 10.1073/pnas.1304594110 · DOI · Paper page
- Chatterjee, 2013, Structural insights into the regulation of cohesion establishment by Wpl1, EMBO J., 32, 677, 10.1038/emboj.2013.16 · DOI
- Holm, 2022, Dali server: structural unification of protein families, Nucleic Acids Res., 50, W210, 10.1093/nar/gkac387 · DOI
- Metsalu, 2015, ClustVis: a web tool for visualizing clustering of multivariate data using Principal Component Analysis and heatmap, Nucleic Acids Res., 43, W566, 10.1093/nar/gkv468 · DOI
- Oldenkamp, 2022, A walk through the SMC cycle: From catching DNAs to shaping the genome, Mol. Cell, 82, 1616, 10.1016/j.molcel.2022.04.006 · DOI
- Taschner, 2021, Nse5/6 inhibits the Smc5/6 ATPase and modulates DNA substrate binding, EMBO J., 40, 10.15252/embj.2021107807 · DOI
- Yu, 2021, Integrative analysis reveals unique structural and functional features of the Smc5/6 complex, Proc. Natl. Acad. Sci. USA, 118, 10.1073/pnas.2026844118 · DOI
- Mallik, 2020, Determining the interaction status and evolutionary fate of duplicated homomeric proteins, PLoS Comput. Biol., 16, 10.1371/journal.pcbi.1008145 · DOI
- Pereira-Leal, 2007, Evolution of protein complexes by duplication of homomeric interactions, Genome Biol., 8, R51, 10.1186/gb-2007-8-4-r51 · DOI
- Mallik, 2025, Co-translational assembly promotes functional diversification of paralogous proteins, bioRxiv
- Després, 2024, Compensatory mutations potentiate constructive neutral evolution by gene duplication, Sci. Technol. Humanit., 385, 770
- Jo, 2021, Structure Basis for Shaping the Nse4 Protein by the Nse1 and Nse3 Dimer within the Smc5/6 Complex, J. Mol. Biol., 433, 10.1016/j.jmb.2021.166910 · DOI
- Ibars, 2023, Ubiquitin proteomics identifies RNA polymerase I as a target of the Smc5/6 complex, Cell Rep., 42, 10.1016/j.celrep.2023.112463 · DOI
- Makarova, 2005, Ancestral paralogs and pseudoparalogs and their role in the emergence of the eukaryotic cell, Nucleic Acids Res., 33, 4626, 10.1093/nar/gki775 · DOI
- Vosseberg, 2021, Timing the origin of eukaryotic cellular complexity with ancient duplications, Nat. Ecol. Evol., 5, 92, 10.1038/s41559-020-01320-z · DOI · Paper page
- Kim, 2022, Condensin DC loads and spreads from recruitment sites to create loop-anchored TADs in C. elegans, eLife, 11, 10.7554/eLife.68745 · DOI
- Das, 2024, Condensin I folds the Caenorhabditis elegans genome, Nat. Genet., 56, 1737, 10.1038/s41588-024-01832-5 · DOI
- Bunnik, 2019, Comparative 3D genome organization in apicomplexan parasites, Proc. Natl. Acad. Sci. USA, 116, 3183, 10.1073/pnas.1810815116 · DOI
- Zhegalova, 2025, Convergent pairs of highly transcribed genes restrict chromatin looping in Dictyostelium discoideum, Nucleic Acids Res., 53, 10.1093/nar/gkaf006 · DOI
- Bi, 2024, Near telomere-to-telomere genome of the model plant Physcomitrium patens, Nat. Plants, 10, 327, 10.1038/s41477-023-01614-7 · DOI
- Kakui, 2020, Fission yeast condensin contributes to interphase chromatin organization and prevents transcription-coupled DNA damage, Genome Biol., 21, 272, 10.1186/s13059-020-02183-0 · DOI
- Solovei, 2024, Spandrels of the cell nucleus, Curr. Opin. Cell Biol., 90, 10.1016/j.ceb.2024.102421 · DOI
- Gibcus, 2018, A pathway for mitotic chromosome formation, Sci. Technol. Humanit., 359
- Imachi, 2020, Isolation of an archaeon at the prokaryote–eukaryote interface, Nature, 577, 519, 10.1038/s41586-019-1916-6 · DOI · Paper page
- Imachi, 2024, Promethearchaeum syntrophicum gen. nov., sp. nov., an anaerobic, obligately syntrophic archaeon, the first isolate of the lineage “Asgard” archaea, and proposal of the new archaeal phylum Promethearchaeota phyl, Int. J. Syst. Evol. Microbiol., 74, 10.1099/ijsem.0.006435 · DOI
- Rodrigues-Oliveira, 2023, Actin cytoskeleton and complex cell architecture in an Asgard archaeon, Nature, 613, 332, 10.1038/s41586-022-05550-y · DOI
- van Hooff, 2023, Towards unraveling the origins of eukaryotic nuclear genome organization, Trends Cell Biol., 33, 820, 10.1016/j.tcb.2023.07.008 · DOI
- Altschul, 1990, Basic local alignment search tool, J. Mol. Biol., 215, 403, 10.1016/S0022-2836(05)80360-2 · DOI · Paper page
- Altschul, 1997, Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res., 25, 3389, 10.1093/nar/25.17.3389 · DOI · Paper page
- Katoh, 2013, MAFFT multiple sequence alignment software version 7: improvements in performance and usability, Mol. Biol. Evol., 30, 772, 10.1093/molbev/mst010 · DOI · Paper page
- Rozewicki, 2019, MAFFT-DASH: integrated protein sequence and structural alignment, Nucleic Acids Res., 47, W5
- Criscuolo, 2010, BMGE (Block Mapping and Gathering with Entropy): a new software for selection of phylogenetic informative regions from multiple sequence alignments, BMC Evol. Biol., 10, 210, 10.1186/1471-2148-10-210 · DOI
- Thomas, 2022, PANTHER: Making genome-scale phylogenetics accessible to all, Protein Sci., 31, 8, 10.1002/pro.4218 · DOI · Paper page
- Hernández-Plaza, 2022, eggNOG 6.0: enabling comparative genomics across 12 535 organisms, Nucleic Acids Res., 51, D389, 10.1093/nar/gkac1022 · DOI
- Zimmermann, 2018, A Completely Reimplemented MPI Bioinformatics Toolkit with a New HHpred Server at its Core, J. Mol. Biol., 430, 2237, 10.1016/j.jmb.2017.12.007 · DOI · Paper page
- Varadi, 2022, AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models, Nucleic Acids Res., 50, D439, 10.1093/nar/gkab1061 · DOI · Paper page
- Parks, 2022, GTDB: an ongoing census of bacterial and archaeal diversity through a phylogenetically consistent, rank normalized and complete genome-based taxonomy, Nucleic Acids Res., 50, D785, 10.1093/nar/gkab776 · DOI · Paper page
- Parks, 2015, CheckM: assessing the quality of microbial genomes recovered from isolates, single cells, and metagenomes, Genome Res., 25, 1043, 10.1101/gr.186072.114 · DOI · Paper page
- Fu, 2012, CD-HIT: accelerated for clustering the next-generation sequencing data, Bioinformatics, 28, 3150, 10.1093/bioinformatics/bts565 · DOI · Paper page
- Capella-Gutiérrez, 2009, trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses, Bioinformatics, 25, 1972, 10.1093/bioinformatics/btp348 · DOI
- Pei, 2014, PROMALS3D: multiple protein sequence alignment enhanced with evolutionary and three-dimensional structural information, Methods Mol. Biol., 1079, 263, 10.1007/978-1-62703-646-7_17 · DOI
- Steinegger, 2019, HH-suite3 for fast remote homology detection and deep protein annotation, BMC Bioinf., 20, 473, 10.1186/s12859-019-3019-7 · DOI · Paper page
- Morris, 2011, clusterMaker: a multi-algorithm clustering plugin for Cytoscape, BMC Bioinf., 12, 436, 10.1186/1471-2105-12-436 · DOI
- Shannon, 2003, Cytoscape: a software environment for integrated models of biomolecular interaction networks, Genome Res., 13, 2498, 10.1101/gr.1239303 · DOI · Paper page
- Zhang, 2005, TM-align: a protein structure alignment algorithm based on the TM-score, Nucleic Acids Res., 33, 2302, 10.1093/nar/gki524 · DOI · Paper page
- Schrödinger, LLC The PyMOL Molecular Graphics System, Version 2.0. Preprint.
- Letunic, 2024, Interactive Tree of Life (iTOL) v6: recent updates to the phylogenetic tree display and annotation tool, Nucleic Acids Res., 52, W78, 10.1093/nar/gkae268 · DOI
- Meng, 2023, UCSF ChimeraX: Tools for structure building and analysis, Protein Sci., 32, 10.1002/pro.4792 · DOI
- Huerta-Cepas, 2016, ETE 3: Reconstruction, Analysis, and Visualization of Phylogenomic Data, Mol. Biol. Evol., 33, 1635, 10.1093/molbev/msw046 · DOI
- Cock, 2009, Biopython: freely available Python tools for computational molecular biology and bioinformatics, Bioinformatics, 25, 1422, 10.1093/bioinformatics/btp163 · DOI · Paper page
- Orchard, 2014, The MIntAct project--IntAct as a common curation platform for 11 molecular interaction databases, Nucleic Acids Res., 42, D358, 10.1093/nar/gkt1115 · DOI
- Mirdita, 2022, ColabFold: making protein folding accessible to all, Nat. Methods, 19, 679, 10.1038/s41592-022-01488-1 · DOI · Paper page
- Rodrigues, 2018, pdb-tools: a swiss army knife for molecular structures, F1000Res., 7, 1961, 10.12688/f1000research.17456.1 · DOI
- Wickham, 2016, Data Analysis, 189, 10.1007/978-3-319-24277-4_9 · DOI
- Waterhouse, 2009, Jalview Version 2—a multiple sequence alignment editor and analysis workbench, Bioinformatics, 25, 1189, 10.1093/bioinformatics/btp033 · DOI
- de Potter, 2023, Uncoupled evolution of the Polycomb system and deep origin of non-canonical PRC1, Commun. Biol., 6, 1144, 10.1038/s42003-023-05501-x · DOI · Paper page
- Stok, 2023, FIRRM/C1orf112 is synthetic lethal with PICH and mediates RAD51 dynamics, Cell Rep., 42, 10.1016/j.celrep.2023.112668 · DOI
- Haering, 2016, SnapShot: SMC Protein Complexes Part I, Cell, 164, 326, 10.1016/j.cell.2015.12.026 · DOI
- Howard-Till, 2013, A single cohesin complex performs mitotic and meiotic functions in the protist tetrahymena, PLoS Genet., 9, 10.1371/journal.pgen.1003418 · DOI
- Ali, 2018, A streamlined cohesin apparatus is sufficient for mitosis and meiosis in the protist Tetrahymena, Chromosoma (Berl.), 127, 421, 10.1007/s00412-018-0673-x · DOI
- Holá, 2021, Kleisin NSE4 of the SMC5/6 complex is necessary for DNA double strand break repair, but not for recovery from DNA damage in Physcomitrella (Physcomitrium patens), Plant Mol. Biol., 107, 355, 10.1007/s11103-020-01115-7 · DOI
- Lelkes, 2023, Characterization of the conserved features of the NSE6 subunit of the Physcomitrium patens SMC5/6 complex, Plant J., 115, 1084, 10.1111/tpj.16282 · DOI
- Yang, 2019, SWITCH 1/DYAD is a WINGS APART-LIKE antagonist that maintains sister chromatid cohesion in meiosis, Nat. Commun., 10, 1755, 10.1038/s41467-019-09759-w · DOI
- Fujiwara, 2013, Spatiotemporal dynamics of condensins I and II: evolutionary insights from the primitive red alga Cyanidioschyzon merolae, Mol. Biol. Cell, 24, 2515, 10.1091/mbc.e13-04-0208 · DOI
- Gabler, 2020, Protein Sequence Analysis Using the MPI Bioinformatics Toolkit, Curr. Protoc. Bioinformatics, 72, 10.1002/cpbi.108 · DOI · Paper page
- Cromer, 2019, Patronus is the elusive plant securin, preventing chromosome separation by antagonizing separase, Proc. Natl. Acad. Sci. USA, 116, 16018, 10.1073/pnas.1906237116 · DOI
- Hagting, 2002, Human securin proteolysis is controlled by the spindle checkpoint and reveals when the APC/C switches from activation by Cdc20 to Cdh1, J. Cell Biol., 157, 1125, 10.1083/jcb.200111001 · DOI
- Luo, 2017, Molecular mechanism for the regulation of yeast separase by securin, Nature, 542, 255, 10.1038/nature21061 · DOI
- Rosen, 2019, Cohesin cleavage by separase is enhanced by a substrate motif distinct from the cleavage site, Nat. Commun., 10, 5189, 10.1038/s41467-019-13209-y · DOI
- Letunic, 2021, Interactive Tree Of Life (iTOL) v5: an online tool for phylogenetic tree display and annotation, Nucleic Acids Res., 49, W293, 10.1093/nar/gkab301 · DOI
- Andrade, 2001, Comparison of ARM and HEAT protein repeats, J. Mol. Biol., 309, 1, 10.1006/jmbi.2001.4624 · DOI
- Kippert, 2009, Highly sensitive detection of individual HEAT and ARM repeats with HHpred and COACH, PLoS One, 4, 10.1371/journal.pone.0007148 · DOI
Metadata
- Authors
- van Hooff, J. J. E., Raas, M. W. D., Tromer, E. C., & Eme, L.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Royal Netherlands Academy of Arts and Sciences (NL)
- University of Groningen (NL)
- Corresponding author
- van Hooff, Jolien J.E.
- Eme, Laura
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2025-07
- Volume
- 44
- Issue
- 7
- Pages
- 115855
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W4411445485
- Cited by
- 18
- References
- 9
- Citations by year
- 2026: 8 · 2025: 5
- FWCI
- 7.08
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Cell Reports (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (publishedVersion, cc-by)
- HAL (submittedVersion)
- HAL (submittedVersion, cc-by)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Socio-Environmental Systems Modeling (submittedVersion, cc-by)
- Funders
- HORIZON EUROPE European Research Council (803151)
- Dutch Research Council (VI.Veni.212.099, VI.Veni.202.223)
- University of Rhode Island
- Okinawa Institute of Science and Technology Graduate University
- European Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Chromosomal and Genetic Variations
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- structural maintenance of chromosomes, SMC complex, condensin II, cohesin, gene duplication, gene loss, eukaryotic evolution, last eukaryotic common ancestor, Asgard archaea, chromosome organization, genome organization
- MeSH terms
- Adenosine Triphosphatases, Archaea, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, Phylogeny, Cell Cycle Proteins, Evolution, Molecular, Gene Duplication, Multiprotein Complexes, Eukaryota
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