[{"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)","image":"/images/cc_by.png","short":"CC BY (4.0)"},"citation":{"mla":"Kelley, Ron, et al. “Toward Community-Driven Visual Proteomics with Large-Scale Cryo-Electron Tomography of Chlamydomonas Reinhardtii.” <i>Molecular Cell</i>, vol. 86, no. 1, Elsevier, 2026, p. 213–230.e7, doi:<a href=\"https://doi.org/10.1016/j.molcel.2025.11.029\">10.1016/j.molcel.2025.11.029</a>.","ista":"Kelley R, Khavnekar S, Righetto RD, Heebner J, Obr M, Zhang X, Chakraborty S, Tagiltsev G, Michael AK, Van Dorst S, Waltz F, Mccafferty CL, Lamm L, Zufferey S, Van Der Stappen P, Van Den Hoek H, Wietrzynski W, Harar P, Wan W, Briggs JAG, Plitzko JM, Engel BD, Kotecha A. 2026. Toward community-driven visual proteomics with large-scale cryo-electron tomography of Chlamydomonas reinhardtii. Molecular Cell. 86(1), 213–230.e7.","apa":"Kelley, R., Khavnekar, S., Righetto, R. D., Heebner, J., Obr, M., Zhang, X., … Kotecha, A. (2026). Toward community-driven visual proteomics with large-scale cryo-electron tomography of Chlamydomonas reinhardtii. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.molcel.2025.11.029\">https://doi.org/10.1016/j.molcel.2025.11.029</a>","chicago":"Kelley, Ron, Sagar Khavnekar, Ricardo D. Righetto, Jessica Heebner, Martin Obr, Xianjun Zhang, Saikat Chakraborty, et al. “Toward Community-Driven Visual Proteomics with Large-Scale Cryo-Electron Tomography of Chlamydomonas Reinhardtii.” <i>Molecular Cell</i>. Elsevier, 2026. <a href=\"https://doi.org/10.1016/j.molcel.2025.11.029\">https://doi.org/10.1016/j.molcel.2025.11.029</a>.","ama":"Kelley R, Khavnekar S, Righetto RD, et al. Toward community-driven visual proteomics with large-scale cryo-electron tomography of Chlamydomonas reinhardtii. <i>Molecular Cell</i>. 2026;86(1):213-230.e7. doi:<a href=\"https://doi.org/10.1016/j.molcel.2025.11.029\">10.1016/j.molcel.2025.11.029</a>","ieee":"R. Kelley <i>et al.</i>, “Toward community-driven visual proteomics with large-scale cryo-electron tomography of Chlamydomonas reinhardtii,” <i>Molecular Cell</i>, vol. 86, no. 1. Elsevier, p. 213–230.e7, 2026.","short":"R. Kelley, S. Khavnekar, R.D. Righetto, J. Heebner, M. Obr, X. Zhang, S. Chakraborty, G. Tagiltsev, A.K. Michael, S. Van Dorst, F. Waltz, C.L. Mccafferty, L. Lamm, S. Zufferey, P. Van Der Stappen, H. Van Den Hoek, W. Wietrzynski, P. Harar, W. Wan, J.A.G. Briggs, J.M. Plitzko, B.D. Engel, A. Kotecha, Molecular Cell 86 (2026) 213–230.e7."},"file_date_updated":"2026-07-28T07:38:45Z","author":[{"last_name":"Kelley","full_name":"Kelley, Ron","first_name":"Ron"},{"last_name":"Khavnekar","first_name":"Sagar","full_name":"Khavnekar, Sagar"},{"last_name":"Righetto","first_name":"Ricardo D.","full_name":"Righetto, Ricardo D."},{"last_name":"Heebner","first_name":"Jessica","full_name":"Heebner, Jessica"},{"last_name":"Obr","first_name":"Martin","full_name":"Obr, Martin","orcid":"0000-0003-1756-6564","id":"4741CA5A-F248-11E8-B48F-1D18A9856A87"},{"full_name":"Zhang, Xianjun","first_name":"Xianjun","last_name":"Zhang"},{"last_name":"Chakraborty","first_name":"Saikat","full_name":"Chakraborty, Saikat"},{"first_name":"Grigory","full_name":"Tagiltsev, Grigory","last_name":"Tagiltsev"},{"last_name":"Michael","first_name":"Alicia","full_name":"Michael, Alicia","orcid":"0000-0002-6080-839X","id":"6437c950-2a03-11ee-914d-d6476dd7b75c"},{"last_name":"Van Dorst","first_name":"Sofie","full_name":"Van Dorst, Sofie"},{"first_name":"Florent","full_name":"Waltz, Florent","last_name":"Waltz"},{"last_name":"Mccafferty","first_name":"Caitlyn L.","full_name":"Mccafferty, Caitlyn L."},{"last_name":"Lamm","full_name":"Lamm, Lorenz","first_name":"Lorenz"},{"first_name":"Simon","full_name":"Zufferey, Simon","last_name":"Zufferey"},{"first_name":"Philippe","full_name":"Van Der Stappen, Philippe","last_name":"Van Der Stappen"},{"full_name":"Van Den Hoek, Hugo","first_name":"Hugo","last_name":"Van Den Hoek"},{"first_name":"Wojciech","full_name":"Wietrzynski, Wojciech","last_name":"Wietrzynski"},{"last_name":"Harar","full_name":"Harar, Pavol","orcid":"0000-0001-5206-1794","id":"e03d953a-6e8c-11ef-99e4-f0717d385cd5","first_name":"Pavol"},{"first_name":"William","full_name":"Wan, William","last_name":"Wan"},{"last_name":"Briggs","full_name":"Briggs, John A.G.","first_name":"John A.G."},{"last_name":"Plitzko","full_name":"Plitzko, Jürgen M.","first_name":"Jürgen M."},{"last_name":"Engel","full_name":"Engel, Benjamin D.","first_name":"Benjamin D."},{"first_name":"Abhay","full_name":"Kotecha, Abhay","last_name":"Kotecha"}],"das_tickbox":"1","type":"journal_article","issue":"1","acknowledgement":"Calculations were performed at the Max Planck Institute of Biochemistry and the Raven Supercomputer of the Max Planck Computing and Data Facility (MPCDF) in Garching, Germany; at the sciCORE (http://scicore.unibas.ch/) scientific computing center at the University of Basel, Switzerland; and at Thermo Fisher Scientific, in Eindhoven, the Netherlands. This work was supported by Thermo Fisher Scientific. All lamella preparations and tilt-series collections used in this work were conducted at Thermo Fisher R&D facilities in Brno and Eindhoven, utilizing Arctis and Krios microscopes. This work was also supported by the ERC consolidator grant “cryOcean” (fulfilled by the Swiss State Secretariat for Education, Research and Innovation, M822.00045) as well as a Swiss Nanoscience Institute PhD school grant to B.D.E. and P.V.d.S., an EMBO long-term postdoctoral fellowship (ALTF-383-2022) to G.T., an SNSF Postdoctoral Fellowship (project 210561) to F.W., a Boehringer Ingelheim Fonds fellowship to L.L., and by the Max Planck Society to J.A.G.B. and J.M.P.","file":[{"success":1,"creator":"dernst","file_id":"22599","file_name":"2026_MolecularCell_Kelley.pdf","date_updated":"2026-07-28T07:38:45Z","file_size":26749637,"date_created":"2026-07-28T07:38:45Z","content_type":"application/pdf","access_level":"open_access","relation":"main_file","checksum":"96a2f8519124d1a0d9de8d2594bf7147"}],"publication_identifier":{"issn":["1097-2765"],"eissn":["1097-4164"]},"volume":86,"language":[{"iso":"eng"}],"oa":1,"page":"213-230.e7","supplementarymaterial":"yes","publisher":"Elsevier","ddc":["570"],"researchdata_availability":"yes","dataavailabilitystatement":"Raw EM data are available at the EMPIAR under accession code EMPIAR: EMPIAR-11830. Annotation and processing information for all 1,829 tomograms are provided in spreadsheet format.153 The following subtomogram averages have been deposited at the Electron Microscopy Data Bank (EMDB): 80S ribosome (EMDB: EMD-51847), nucleosome (EMDB: EMD-19906), PSII (EMDB: EMD-51731), Rubisco (EMDB: EMD-51848), microtubule (EMDB: EMD-51804), clathrin (EMDB: EMD-51789), and ATP synthase (EMDB: EMD-51802). Segmentations shown in Figures 2 and 3 are deposited on Zenodo (https://doi.org/10.5281/zenodo.15875785). Particle positions and orientations used for STA, along with all resources derived from this work, are available on GitHub (https://github.com/Chromatin-Structure-Rhythms-Lab/ChlamyAnnotations). Reconstructed tomograms and annotations are also available to explore interactively at the CZII Cryo-ET Data Portal (DS-10302, https://cryoetdataportal.czscience.com/datasets/10302/). Raw data for cryo-PFIB/SEM slice-and-view of a whole C. reinhardtii cell has also been deposited (EMPIAR: EMPIAR-11275).\r\n\r\nThis paper does not report original code.\r\n\r\nAny additional information required to reanalyze the data reported in this paper is available from the lead contact upon request.","department":[{"_id":"AlMi"}],"oa_version":"Published Version","PlanS_conform":"1","abstract":[{"lang":"eng","text":"In situ cryo-electron tomography (cryo-ET) has emerged as the method of choice to investigate the structures of biomolecules in their native context. However, challenges remain for the efficient production and sharing of large-scale cryo-ET datasets. Here, we combined cryogenic plasma-based focused ion beam (cryo-PFIB) milling with recent advances in cryo-ET acquisition and processing to generate a dataset of 1,829 annotated tomograms of the green alga Chlamydomonas reinhardtii, which we provide as a community resource to drive method development and inspire biological discovery. To assay data quality, we performed subtomogram averaging of both soluble and membrane-bound complexes ranging in size from >3 MDa to ∼200 kDa, including 80S ribosomes, Rubisco, nucleosomes, microtubules, clathrin, photosystem II, and mitochondrial ATP synthase. The majority of these density maps reached sub-nanometer resolution, demonstrating the potential of this C. reinhardtii dataset as well as the promise of modern cryo-ET workflows and open data sharing to empower visual proteomics."}],"_id":"20935","status":"public","day":"08","month":"01","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","title":"Toward community-driven visual proteomics with large-scale cryo-electron tomography of Chlamydomonas reinhardtii","OA_type":"hybrid","has_accepted_license":"1","OA_place":"publisher","year":"2026","article_type":"original","date_created":"2026-01-04T23:01:36Z","publication_status":"published","doi":"10.1016/j.molcel.2025.11.029","fulldoi":"https://doi.org/10.1016/j.molcel.2025.11.029","article_processing_charge":"Yes (in subscription journal)","scopus_import":"1","publication":"Molecular Cell","date_published":"2026-01-08T00:00:00Z","intvolume":"        86","date_updated":"2026-07-28T07:39:23Z","quality_controlled":"1"},{"type":"journal_article","das_tickbox":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1016/j.molcel.2026.05.026"}],"citation":{"apa":"Zhao, Z., &#38; Sazanov, L. A. (n.d.). Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.molcel.2026.05.026\">https://doi.org/10.1016/j.molcel.2026.05.026</a>","ista":"Zhao Z, Sazanov LA. Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo. Molecular Cell.","mla":"Zhao, Ziyu, and Leonid A. Sazanov. “Structure of E. Coli Twin-Arginine Translocase (Tat) Complex with Bound Cargo.” <i>Molecular Cell</i>, Elsevier, doi:<a href=\"https://doi.org/10.1016/j.molcel.2026.05.026\">10.1016/j.molcel.2026.05.026</a>.","chicago":"Zhao, Ziyu, and Leonid A Sazanov. “Structure of E. Coli Twin-Arginine Translocase (Tat) Complex with Bound Cargo.” <i>Molecular Cell</i>. Elsevier, n.d. <a href=\"https://doi.org/10.1016/j.molcel.2026.05.026\">https://doi.org/10.1016/j.molcel.2026.05.026</a>.","ama":"Zhao Z, Sazanov LA. Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo. <i>Molecular Cell</i>. doi:<a href=\"https://doi.org/10.1016/j.molcel.2026.05.026\">10.1016/j.molcel.2026.05.026</a>","ieee":"Z. Zhao and L. A. Sazanov, “Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo,” <i>Molecular Cell</i>. Elsevier.","short":"Z. Zhao, L.A. Sazanov, Molecular Cell (n.d.)."},"tmp":{"name":"Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)","legal_code_url":"https://creativecommons.org/licenses/by-nc/4.0/legalcode","short":"CC BY-NC (4.0)","image":"/images/cc_by_nc.png"},"author":[{"id":"a63fe682-9f3a-11ee-bf8c-cfdf919b9850","full_name":"Zhao, Ziyu","first_name":"Ziyu","last_name":"Zhao"},{"last_name":"Sazanov","first_name":"Leonid A","id":"338D39FE-F248-11E8-B48F-1D18A9856A87","full_name":"Sazanov, Leonid A","orcid":"0000-0002-0977-7989"}],"acknowledged_ssus":[{"_id":"EM-Fac"},{"_id":"ScienComp"}],"license":"https://creativecommons.org/licenses/by-nc/4.0/","publisher":"Elsevier","supplementarymaterial":"yes","researchdata_availability":"yes","ddc":["570"],"oa":1,"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["1097-4164"],"issn":["1097-2765"]},"biorxivid":1,"acknowledgement":"We thank IST Austria for providing the funding. We thank IST Austria EM facility for the use of Titan Krios TEM. Data processing was performed using IST high-performance computer cluster. We thank Dr. R. Roemhild and Professor C. Guet (ISTA) for help in constructing Tat deletion strains and Dr. A. Charnagalov (ISTA) for technical help.","title":"Structure of E. Coli twin-arginine translocase (Tat) complex with bound cargo","user_id":"ba8df636-2132-11f1-aed0-ed93e2281fdd","OA_type":"hybrid","OA_place":"publisher","has_accepted_license":"1","related_material":{"record":[{"status":"public","relation":"research_data","id":"22189"}],"link":[{"relation":"press_release","description":"News on ISTA website","url":"https://ista.ac.at/en/news/the-gate-for-bulky-cargo/"}]},"month":"06","day":"22","status":"public","corr_author":"1","department":[{"_id":"LeSa"}],"abstract":[{"lang":"eng","text":"How the twin-arginine translocase (Tat) system transports fully folded substrate proteins across cellular membranes without disrupting membrane integrity has been a fundamental question in cell biology for decades. The Tat system, found in prokaryotes and plant organelles, recognizes a cargo signal peptide via a conserved twin-arginine motif. The multi-subunit Tat complex facilitates the proton-motive-force-dependent translocation process, yet its overall architecture has remained unknown. Here, we present the cryo-electron microscopy (cryo-EM) structure of the Escherichia coli (E. coli) trimeric TatB₃C₃ complex with bound substrate SufI, assembled in vivo. The complex adopts an unusual, wide-open, bowl-shaped architecture with a polar inner cavity. Unexpectedly, the cargo is engaged in a dual-contact mode: while the signal peptide binds inside one TatBC unit, the folded domain docks tightly onto an adjacent unit, possibly performing a proofreading function. This structure provides a mechanistic framework for substrate engagement and suggests the direct involvement of the entire Tat complex in substrate translocation."}],"_id":"22148","oa_version":"Published Version","external_id":{"biorxivid":["10.1101/2025.09.16.676506"]},"dataavailabilitystatement":"This study did not generate new unique reagents. Strains and plasmids generated in this study are available from the lead contact without restrictions.\r\n• Source data are provided within this paper. The cryo-EM map is deposited in the Electron Microscopy Data Bank under accession number EMD-53848. The model is deposited in the Protein Data Bank under accession number 9R91. The structural data are publicly available as of the date of publication. Raw images of spot assays, SDS-PAGE and BN-PAGE gels with Coomassie staining and immunoblot images are available at Mendeley Data (https://doi.org/10.17632/v2g3p9n985.1).\r\n• This paper does not report original code.\r\n• Any additional information required to reanalyze the data reported in this paper is available from the lead contact upon request.","date_updated":"2026-08-12T12:08:44Z","quality_controlled":"1","publication":"Molecular Cell","date_published":"2026-06-22T00:00:00Z","fulldoi":"https://doi.org/10.1016/j.molcel.2026.05.026","doi":"10.1016/j.molcel.2026.05.026","article_processing_charge":"Yes (via OA deal)","scopus_import":"1","year":"2026","publication_status":"inpress","date_created":"2026-06-28T22:01:35Z","article_type":"original"},{"scopus_import":"1","article_processing_charge":"Yes (in subscription journal)","fulldoi":"https://doi.org/10.1016/j.molcel.2024.07.022","doi":"10.1016/j.molcel.2024.07.022","publication_status":"published","date_created":"2024-09-15T22:01:41Z","article_type":"original","year":"2024","quality_controlled":"1","date_updated":"2026-09-24T10:43:18Z","intvolume":"        84","date_published":"2024-09-05T00:00:00Z","publication":"Molecular Cell","pmid":1,"_id":"18072","abstract":[{"lang":"eng","text":"The individualization of chromosomes during early mitosis and their clustering upon exit from cell division are two key transitions that ensure efficient segregation of eukaryotic chromosomes. Both processes are regulated by the surfactant-like protein Ki-67, but how Ki-67 achieves these diametric functions has remained unknown. Here, we report that Ki-67 radically switches from a chromosome repellent to a chromosome attractant during anaphase in human cells. We show that Ki-67 dephosphorylation during mitotic exit and the simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface. Experiments and coarse-grained simulations support a model in which the coalescence of chromosome surfaces, driven by co-condensation of Ki-67 and RNA, promotes clustering of chromosomes. Our study reveals how the switch of Ki-67 from a surfactant to a liquid-like condensed phase can generate mechanical forces during genome segregation that are required for re-establishing nuclear-cytoplasmic compartmentalization after mitosis."}],"ec_funded":1,"oa_version":"Published Version","department":[{"_id":"AnSa"}],"project":[{"name":"Non-Equilibrium Protein Assembly: from Building Blocks to Biological Machines","call_identifier":"H2020","_id":"eba2549b-77a9-11ec-83b8-a81e493eae4e","grant_number":"802960"}],"dataavailabilitystatement":"Raw image files of all figures have been deposited at Mendeley Data and are publicly available as of the date of publication (Mendeley data: https://doi.org/10.17632/dwcpnncsyd.1). All other data reported in this paper will be shared by the lead contact upon request","external_id":{"isi":["001309051100001"],"pmid":["39153474"]},"has_accepted_license":"1","title":"A liquid-like coat mediates chromosome clustering during mitotic exit","user_id":"317138e5-6ab7-11ef-aa6d-ffef3953e345","day":"05","related_material":{"record":[{"id":"22987","relation":"research_data","status":"public"}]},"month":"09","status":"public","isi":1,"volume":84,"publication_identifier":{"eissn":["1097-4164"],"issn":["1097-2765"]},"file":[{"checksum":"3f360e0287b8ec79fb2b8b02b5070360","relation":"main_file","date_created":"2024-09-16T07:38:38Z","access_level":"open_access","content_type":"application/pdf","file_size":11654644,"file_name":"2024_MolecularCell_HernandezArmendariz.pdf","date_updated":"2024-09-16T07:38:38Z","creator":"dernst","file_id":"18075","success":1}],"acknowledgement":"We thank Daniel W. Gerlich for providing cell lines, the EMBL Advanced Light Microscopy Facility (ALMF) for support, Christian H. Haering and Thomas Quail for input on the manuscript, and Martina Dees for cloning several Ki-67 constructs. This work was supported by the German Research Foundation (DFG project number 402723784) and the Human Frontier Science Program (CDA00045/2019). A.H.-A. and A.B. have received PhD fellowships from the Boehringer Ingelheim Fonds, V.S. and A.Š. were supported by the European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation programme (grant no. 802960), and Y.H. was supported by a fellowship from the EMBL interdisciplinary Postdoc (EIPOD) program (Marie Sklodowska-Curie Actions, COFUND grant agreement 664726).","researchdata_availability":"yes","ddc":["570"],"publisher":"Cell Press","supplementarymaterial":"yes","page":"P3254-3270.E9","oa":1,"language":[{"iso":"eng"}],"author":[{"last_name":"Hernandez-Armendariz","first_name":"Alberto","full_name":"Hernandez-Armendariz, Alberto"},{"first_name":"Valerio","id":"ef8a92cb-c7b6-11ec-8bea-e1fd5847bc5b","full_name":"Sorichetti, Valerio","orcid":"0000-0002-9645-6576","last_name":"Sorichetti"},{"last_name":"Hayashi","full_name":"Hayashi, Yuki","first_name":"Yuki"},{"last_name":"Koskova","full_name":"Koskova, Zuzana","first_name":"Zuzana"},{"full_name":"Brunner, Andreas","first_name":"Andreas","last_name":"Brunner"},{"last_name":"Ellenberg","full_name":"Ellenberg, Jan","first_name":"Jan"},{"last_name":"Šarić","full_name":"Šarić, Anđela","orcid":"0000-0002-7854-2139","id":"bf63d406-f056-11eb-b41d-f263a6566d8b","first_name":"Anđela"},{"last_name":"Cuylen-Haering","full_name":"Cuylen-Haering, Sara","first_name":"Sara"}],"file_date_updated":"2024-09-16T07:38:38Z","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)","image":"/images/cc_by.png","short":"CC BY (4.0)"},"citation":{"ama":"Hernandez-Armendariz A, Sorichetti V, Hayashi Y, et al. A liquid-like coat mediates chromosome clustering during mitotic exit. <i>Molecular Cell</i>. 2024;84(17):P3254-3270.E9. doi:<a href=\"https://doi.org/10.1016/j.molcel.2024.07.022\">10.1016/j.molcel.2024.07.022</a>","ieee":"A. Hernandez-Armendariz <i>et al.</i>, “A liquid-like coat mediates chromosome clustering during mitotic exit,” <i>Molecular Cell</i>, vol. 84, no. 17. Cell Press, p. P3254–3270.E9, 2024.","short":"A. Hernandez-Armendariz, V. Sorichetti, Y. Hayashi, Z. Koskova, A. Brunner, J. Ellenberg, A. Šarić, S. Cuylen-Haering, Molecular Cell 84 (2024) P3254–3270.E9.","apa":"Hernandez-Armendariz, A., Sorichetti, V., Hayashi, Y., Koskova, Z., Brunner, A., Ellenberg, J., … Cuylen-Haering, S. (2024). A liquid-like coat mediates chromosome clustering during mitotic exit. <i>Molecular Cell</i>. Cell Press. <a href=\"https://doi.org/10.1016/j.molcel.2024.07.022\">https://doi.org/10.1016/j.molcel.2024.07.022</a>","ista":"Hernandez-Armendariz A, Sorichetti V, Hayashi Y, Koskova Z, Brunner A, Ellenberg J, Šarić A, Cuylen-Haering S. 2024. A liquid-like coat mediates chromosome clustering during mitotic exit. Molecular Cell. 84(17), P3254–3270.E9.","mla":"Hernandez-Armendariz, Alberto, et al. “A Liquid-like Coat Mediates Chromosome Clustering during Mitotic Exit.” <i>Molecular Cell</i>, vol. 84, no. 17, Cell Press, 2024, p. P3254–3270.E9, doi:<a href=\"https://doi.org/10.1016/j.molcel.2024.07.022\">10.1016/j.molcel.2024.07.022</a>.","chicago":"Hernandez-Armendariz, Alberto, Valerio Sorichetti, Yuki Hayashi, Zuzana Koskova, Andreas Brunner, Jan Ellenberg, Anđela Šarić, and Sara Cuylen-Haering. “A Liquid-like Coat Mediates Chromosome Clustering during Mitotic Exit.” <i>Molecular Cell</i>. Cell Press, 2024. <a href=\"https://doi.org/10.1016/j.molcel.2024.07.022\">https://doi.org/10.1016/j.molcel.2024.07.022</a>."},"type":"journal_article","issue":"17","das_tickbox":"1"},{"external_id":{"pmid":["31732458"]},"department":[{"_id":"DaZi"}],"oa_version":"Published Version","_id":"9526","abstract":[{"text":"DNA methylation and histone H1 mediate transcriptional silencing of genes and transposable elements, but how they interact is unclear. In plants and animals with mosaic genomic methylation, functionally mysterious methylation is also common within constitutively active housekeeping genes. Here, we show that H1 is enriched in methylated sequences, including genes, of Arabidopsis thaliana, yet this enrichment is independent of DNA methylation. Loss of H1 disperses heterochromatin, globally alters nucleosome organization, and activates H1-bound genes, but only weakly de-represses transposable elements. However, H1 loss strongly activates transposable elements hypomethylated through mutation of DNA methyltransferase MET1. Hypomethylation of genes also activates antisense transcription, which is modestly enhanced by H1 loss. Our results demonstrate that H1 and DNA methylation jointly maintain transcriptional homeostasis by silencing transposable elements and aberrant intragenic transcripts. Such functionality plausibly explains why DNA methylation, a well-known mutagen, has been maintained within coding sequences of crucial plant and animal genes.","lang":"eng"}],"status":"public","month":"01","day":"16","user_id":"0043cee0-e5fc-11ee-9736-f83bc23afbf0","title":"DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts","OA_type":"hybrid","OA_place":"publisher","extern":"1","year":"2020","date_created":"2021-06-08T06:37:09Z","article_type":"original","publication_status":"published","doi":"10.1016/j.molcel.2019.10.011","fulldoi":"https://doi.org/10.1016/j.molcel.2019.10.011","article_processing_charge":"No","scopus_import":"1","pmid":1,"publication":"Molecular Cell","date_published":"2020-01-16T00:00:00Z","intvolume":"        77","quality_controlled":"1","date_updated":"2024-10-16T12:14:37Z","citation":{"ista":"Choi J, Lyons DB, Kim MY, Moore JD, Zilberman D. 2020. DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts. Molecular Cell. 77(2), 310–323.e7.","mla":"Choi, Jaemyung, et al. “DNA Methylation and Histone H1 Jointly Repress Transposable Elements and Aberrant Intragenic Transcripts.” <i>Molecular Cell</i>, vol. 77, no. 2, Elsevier, 2020, p. 310–323.e7, doi:<a href=\"https://doi.org/10.1016/j.molcel.2019.10.011\">10.1016/j.molcel.2019.10.011</a>.","apa":"Choi, J., Lyons, D. B., Kim, M. Y., Moore, J. D., &#38; Zilberman, D. (2020). DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts. <i>Molecular Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.molcel.2019.10.011\">https://doi.org/10.1016/j.molcel.2019.10.011</a>","chicago":"Choi, Jaemyung, David B. Lyons, M. Yvonne Kim, Jonathan D. Moore, and Daniel Zilberman. “DNA Methylation and Histone H1 Jointly Repress Transposable Elements and Aberrant Intragenic Transcripts.” <i>Molecular Cell</i>. Elsevier, 2020. <a href=\"https://doi.org/10.1016/j.molcel.2019.10.011\">https://doi.org/10.1016/j.molcel.2019.10.011</a>.","ama":"Choi J, Lyons DB, Kim MY, Moore JD, Zilberman D. DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts. <i>Molecular Cell</i>. 2020;77(2):310-323.e7. doi:<a href=\"https://doi.org/10.1016/j.molcel.2019.10.011\">10.1016/j.molcel.2019.10.011</a>","ieee":"J. Choi, D. B. Lyons, M. Y. Kim, J. D. Moore, and D. Zilberman, “DNA methylation and histone H1 jointly repress transposable elements and aberrant intragenic transcripts,” <i>Molecular Cell</i>, vol. 77, no. 2. Elsevier, p. 310–323.e7, 2020.","short":"J. Choi, D.B. Lyons, M.Y. Kim, J.D. Moore, D. Zilberman, Molecular Cell 77 (2020) 310–323.e7."},"author":[{"last_name":"Choi","first_name":"Jaemyung","full_name":"Choi, Jaemyung"},{"full_name":"Lyons, David B.","first_name":"David B.","last_name":"Lyons"},{"last_name":"Kim","first_name":"M. Yvonne","full_name":"Kim, M. Yvonne"},{"last_name":"Moore","first_name":"Jonathan D.","full_name":"Moore, Jonathan D."},{"last_name":"Zilberman","first_name":"Daniel","orcid":"0000-0002-0123-8649","full_name":"Zilberman, Daniel","id":"6973db13-dd5f-11ea-814e-b3e5455e9ed1"}],"issue":"2","type":"journal_article","main_file_link":[{"url":"https://doi.org/10.1016/j.molcel.2019.10.011","open_access":"1"}],"publication_identifier":{"issn":["1097-2765"],"eissn":["1097-4164"]},"volume":77,"oa":1,"language":[{"iso":"eng"}],"page":"310-323.e7","publisher":"Elsevier"}]