The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural features of nucleosomes in interphase and metaphase chromosomes
Open accessPublished version of a preprint
Abstract
Structural heterogeneity of nucleosomes in functional chromosomes is unknown. Here, we devise the template-, reference- and selection-free (TRSF) cryo-EM pipeline to simultaneously reconstruct cryo-EM structures of protein complexes from interphase or metaphase chromosomes. The reconstructed interphase and metaphase nucleosome structures are on average indistinguishable from canonical nucleosome structures, despite DNA sequence heterogeneity, cell-cycle-specific posttranslational modifications, and interacting proteins. Nucleosome structures determined by a decoy-classifying method and structure variability analyses reveal the nucleosome structural variations in linker DNA, histone tails, and nucleosome core particle configurations, suggesting that the opening of linker DNA, which is correlated with H2A C-terminal tail positioning, is suppressed in chromosomes. High-resolution (3.4-3.5 Å) nucleosome structures indicate DNA-sequence-independent stabilization of superhelical locations ±0-1 and ±3.5-4.5. The linker histone H1.8 preferentially binds to metaphase chromatin, from which chromatosome cryo-EM structures with H1.8 at the on-dyad position are reconstituted. This study presents the structural characteristics of nucleosomes in chromosomes.
Overview
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
Verification
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.
Citations
Cites
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function
Dodonova, S. O., Zhu, F., Dienemann, C., Taipale, J., & Cramer, P. (2020) · Nature · doi:10.1038/s41586-020-2195-y · Cited by 265
Flagged first, then by citations
Research works printed but not linked: 135
- Adams, 1995, Binding of disparate transcriptional activators to nucleosomal DNA is inherently cooperative, Mol. Cell. Biol., 15, 1405, 10.1128/MCB.15.3.1405 · DOI
- Adhireksan, 2020, Near-atomic resolution structures of interdigitated nucleosome fibres, Nat. Commun., 11, 4747, 10.1038/s41467-020-18533-2 · DOI
- Ali-Ahmad, 2019, CENP-C unwraps the human CENP-A nucleosome through the H2A C-terminal tail, EMBO Rep., 20, e48913, 10.15252/embr.201948913 · DOI
- An, 1998, Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner, Proc. Natl. Acad. Sci. USA, 95, 3396, 10.1073/pnas.95.7.3396 · DOI
- Arimura, 2012, Structural analysis of the hexasome, lacking one histone H2A/H2B dimer from the conventional nucleosome, Biochemistry, 51, 3302, 10.1021/bi300129b · DOI
- Arimura, 2018, Cancer-associated mutations of histones H2B, H3.1 and H2A.Z.1 affect the structure and stability of the nucleosome, Nucleic Acids Res., 46, 10007
- Arimura, 2019, The CENP-A centromere targeting domain facilitates H4K20 monomethylation in the nucleosome by structural polymorphism, Nat. Commun., 10, 576, 10.1038/s41467-019-08314-x · DOI
- Armache, 2019, Cryo-EM structures of remodeler-nucleosome intermediates suggest allosteric control through the nucleosome, eLife, 8, 1, 10.7554/eLife.46057 · DOI
- Ayala, 2018, Structure and regulation of the human INO80-nucleosome complex, Nature, 556, 391, 10.1038/s41586-018-0021-6 · DOI
- Baker, 2001, Electrostatics of nanosystems: application to microtubules and the ribosome, Proc. Natl. Acad. Sci. USA, 98, 10037, 10.1073/pnas.181342398 · DOI
- Bancaud, 2007, Nucleosome chiral transition under positive torsional stress in single chromatin fibers, Mol. Cell, 27, 135, 10.1016/j.molcel.2007.05.037 · DOI
- Basu, 2021, Measuring DNA mechanics on the genome scale, Nature, 589, 462, 10.1038/s41586-020-03052-3 · DOI
- Bednar, 2017, Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1, Mol. Cell, 66, 384, 10.1016/j.molcel.2017.04.012 · DOI
- Bell, 2016, High resolution single particle refinement in EMAN2.1, Methods, 100, 25, 10.1016/j.ymeth.2016.02.018 · DOI
- Bepler, 2019, Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs, Nat. Methods, 16, 1153, 10.1038/s41592-019-0575-8 · DOI
- Buckwalter, 2017, Regulation of chromatin folding by conformational variations of nucleosome linker DNA, Nucleic Acids Res., 45, 9372, 10.1093/nar/gkx562 · DOI
- Cai, 2018, Cryo-ET reveals the macromolecular reorganization of S. pombe mitotic chromosomes in vivo, Proc. Natl. Acad. Sci. USA, 115, 10977, 10.1073/pnas.1720476115 · DOI
- Cai, 2018, The in situ structures of mono-, di-, and trinucleosomes in human heterochromatin, Mol. Biol. Cell, 29, 2450, 10.1091/mbc.E18-05-0331 · DOI
- Cardone, 2013, One number does not fit all: mapping local variations in resolution in cryo-EM reconstructions, J. Struct. Biol., 184, 226, 10.1016/j.jsb.2013.08.002 · DOI
- Chen, 2017, Regulation of Nucleosome Stacking and Chromatin Compaction by the Histone H4 N-Terminal Tail-H2A Acidic Patch Interaction, J. Mol. Biol., 429, 2075, 10.1016/j.jmb.2017.03.016 · DOI
- Chicano, 2019, Frozen-hydrated chromatin from metaphase chromosomes has an interdigitated multilayer structure, EMBO J., 38, 1, 10.15252/embj.201899769 · DOI
- Choppakatla, 2021, Linker histone H1.8 inhibits chromatin-binding of condensins and DNA topoisomerase II to tune chromosome length and individualization, eLife, 10, e68918, 10.7554/eLife.68918 · DOI
- Chua, 2012, The mechanics behind DNA sequence-dependent properties of the nucleosome, Nucleic Acids Res., 40, 6338, 10.1093/nar/gks261 · DOI
- Chua, 2016, 3.9 Å structure of the nucleosome core particle determined by phase-plate cryo-EM, Nucleic Acids Res., 44, 8013, 10.1093/nar/gkw708 · DOI
- Corujo, 2018, Post-translational modifications of H2A histone variants and their role in cancer, Cancers (Basel), 10, 1, 10.3390/cancers10030059 · DOI
- D’Imprima, 2019, Protein denaturation at the air-water interface and how to prevent it, eLife, 8, 1
- de la Rosa-Trevín, 2016, Scipion: a software framework toward integration, reproducibility and validation in 3D electron microscopy, J. Struct. Biol., 195, 93, 10.1016/j.jsb.2016.04.010 · DOI
- Dolinsky, 2004, PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations, Nucleic Acids Res., 32, W665, 10.1093/nar/gkh381 · DOI
- Dorigo, 2004, Nucleosome arrays reveal the two-start organization of the chromatin fiber, Science, 306, 1571, 10.1126/science.1103124 · DOI
- Dworkin-Rastl, 1994, The maternal histone H1 variant, H1M (B4 protein), is the predominant H1 histone in Xenopus pregastrula embryos, Dev. Biol., 161, 425, 10.1006/dbio.1994.1042 · DOI
- Ekundayo, 2017, Capturing Structural Heterogeneity in Chromatin Fibers, J. Mol. Biol., 429, 3031, 10.1016/j.jmb.2017.09.002 · DOI
- Eltsov, 2008, Analysis of cryo-electron microscopy images does not support the existence of 30-nm chromatin fibers in mitotic chromosomes in situ, Proc. Natl. Acad. Sci. USA, 105, 19732, 10.1073/pnas.0810057105 · DOI
- Eltsov, 2018, Nucleosome conformational variability in solution and in interphase nuclei evidenced by cryo-electron microscopy of vitreous sections, Nucleic Acids Res., 46, 9189, 10.1093/nar/gky670 · DOI
- Emsley, 2004, Coot: model-building tools for molecular graphics, Acta Crystallogr. D Biol. Crystallogr., 60, 2126, 10.1107/S0907444904019158 · DOI · Paper page
- Eustermann, 2018, Structural basis for ATP-dependent chromatin remodelling by the INO80 complex, Nature, 556, 386, 10.1038/s41586-018-0029-y · DOI
- Falk, 2015, CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere, Science, 348, 699, 10.1126/science.1259308 · DOI
- Farnung, 2017, Nucleosome-Chd1 structure and implications for chromatin remodelling, Nature, 550, 539, 10.1038/nature24046 · DOI
- Fujii, 2010, Direct visualization of secondary structures of F-actin by electron cryomicroscopy, Nature, 467, 724, 10.1038/nature09372 · DOI
- Funabiki, 2017, Nucleosome-Dependent Pathways That Control Mitotic Progression, Cold Spring Harb. Symp. Quant. Biol., 82, 173, 10.1101/sqb.2017.82.034512 · DOI
- Furuyama, 2013, Reconstitution of hemisomes on budding yeast centromeric DNA, Nucleic Acids Res., 41, 5769, 10.1093/nar/gkt314 · DOI
- Gagnon, 2015, Undetectable histone O-GlcNAcylation in mammalian cells, Epigenetics, 10, 677, 10.1080/15592294.2015.1060387 · DOI
- Gibbs, 2018, Linker histones as liquid-like glue for chromatin, Proc. Natl. Acad. Sci. USA, 115, 11868, 10.1073/pnas.1816936115 · DOI
- Gibcus, 2018, A pathway for mitotic chromosome formation, Science, 359, eaao6135, 10.1126/science.aao6135 · DOI
- Gibson, 2019, Organization of Chromatin by Intrinsic and Regulated Phase Separation, Cell, 179, 470, 10.1016/j.cell.2019.08.037 · DOI
- Glotzer, 1991, Cyclin is degraded by the ubiquitin pathway, Nature, 349, 132, 10.1038/349132a0 · DOI
- Goloborodko, 2016, Compaction and segregation of sister chromatids via active loop extrusion, eLife, 5, 1, 10.7554/eLife.14864 · DOI
- Gong, 2016, Structural insights into the Niemann-Pick C1 (NPC1)-mediated cholesterol transfer and ebola infection, Cell, 165, 1467, 10.1016/j.cell.2016.05.022 · DOI
- Grigoryev, 2018, Chromatin Higher-Order Folding: A Perspective with Linker DNA Angles, Biophys. J., 114, 2290, 10.1016/j.bpj.2018.03.009 · DOI
- Grigoryev, 2009, Evidence for heteromorphic chromatin fibers from analysis of nucleosome interactions, Proc. Natl. Acad. Sci. USA, 106, 13317, 10.1073/pnas.0903280106 · DOI
- Hall, 2009, High-resolution dynamic mapping of histone-DNA interactions in a nucleosome, Nat. Struct. Mol. Biol., 16, 124, 10.1038/nsmb.1526 · DOI
- Han, 2020, Cryo-EM structure of SWI/SNF complex bound to a nucleosome, Nature, 579, 452, 10.1038/s41586-020-2087-1 · DOI
- Hayashi-Takanaka, 2015, Distribution of histone H4 modifications as revealed by a panel of specific monoclonal antibodies, Chromosome Res., 23, 753, 10.1007/s10577-015-9486-4 · DOI
- He, 2020, Structure of nucleosome-bound human BAF complex, Science, 367, 875, 10.1126/science.aaz9761 · DOI
- Herrero Del Valle, 2020, Prospects for antimicrobial development in the cryo-EM era - a focus on the ribosome, FEMS Microbiol. Rev., 44, 793, 10.1093/femsre/fuaa032 · DOI
- Hirano, 2014, Condensins and the evolution of torsion-mediated genome organization, Trends Cell Biol., 24, 727, 10.1016/j.tcb.2014.06.007 · DOI
- Hirano, 1994, A heterodimeric coiled-coil protein required for mitotic chromosome condensation in vitro, Cell, 79, 449, 10.1016/0092-8674(94)90254-2 · DOI
- Hite, 2017, Structural Titration of Slo2.2, a Na+-Dependent K+ Channel, Cell, 168, 390, 10.1016/j.cell.2016.12.030 · DOI
- Ho, 2021, Structural basis of nucleosomal histone H4 lysine 20 methylation by SET8 methyltransferase, Life Sci. Alliance, 4, e202000919, 10.26508/lsa.202000919 · DOI
- Hyman, 1991, Preparation of modified tubulins, 478, 10.1016/0076-6879(91)96041-O · DOI
- Jenness, 2018, HELLS and CDCA7 comprise a bipartite nucleosome remodeling complex defective in ICF syndrome, Proc. Natl. Acad. Sci. USA, 115, E876, 10.1073/pnas.1717509115 · DOI
- Kastritis, 2017, Capturing protein communities by structural proteomics in a thermophilic eukaryote, Mol. Syst. Biol., 13, 936, 10.15252/msb.20167412 · DOI
- Kato, 2017, Crystal structure of the overlapping dinucleosome composed of hexasome and octasome, Science, 356, 205, 10.1126/science.aak9867 · DOI
- Kelly, 1989, Glycosylation of chromosomal proteins: localization of O-linked N-acetylglucosamine in Drosophila chromatin, Cell, 57, 243, 10.1016/0092-8674(89)90962-8 · DOI
- Kelly, 2010, Survivin reads phosphorylated histone H3 threonine 3 to activate the mitotic kinase Aurora B, Science, 330, 235, 10.1126/science.1189505 · DOI
- Klug, 1980, A low resolution structure for the histone core of the nucleosome, Nature, 287, 509, 10.1038/287509a0 · DOI
- Koslover, 2010, Local geometry and elasticity in compact chromatin structure, Biophys. J., 99, 3941, 10.1016/j.bpj.2010.10.024 · DOI
- Krietenstein, 2020, Mesoscale organization of the chromatin fiber, Curr. Opin. Genet. Dev., 61, 32, 10.1016/j.gde.2020.02.022 · DOI
- Kujirai, 2018, Structural basis of the nucleosome transition during RNA polymerase II passage, Science, 362, 595, 10.1126/science.aau9904 · DOI
- Kyrilis, 2019, Integrative biology of native cell extracts: a new era for structural characterization of life processes, Biol. Chem., 400, 831, 10.1515/hsz-2018-0445 · DOI
- Kyte, 1982, A simple method for displaying the hydropathic character of a protein, J. Mol. Biol., 157, 105, 10.1016/0022-2836(82)90515-0 · DOI
- Lavelle, 2007, Chromatin polymorphism and the nucleosome superfamily: a genealogy, Cell Cycle, 6, 2113, 10.4161/cc.6.17.4631 · DOI
- Liebschner, 2019, Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix, Acta Crystallogr. D Struct. Biol., 75, 861, 10.1107/S2059798319011471 · DOI · Paper page
- Lilic, 2020, The antibiotic sorangicin A inhibits promoter DNA unwinding in a Mycobacterium tuberculosis rifampicin-resistant RNA polymerase, Proc. Natl. Acad. Sci. USA, 117, 30423, 10.1073/pnas.2013706117 · DOI
- Liu, 2017, Mechanism of chromatin remodelling revealed by the Snf2-nucleosome structure, Nature, 544, 440, 10.1038/nature22036 · DOI
- Luger, 1997, Crystal structure of the nucleosome core particle at 2.8 A resolution, Nature, 389, 251, 10.1038/38444 · DOI · Paper page
- Lyumkis, 2013, Likelihood-based classification of cryo-EM images using FREALIGN, J. Struct. Biol., 183, 377, 10.1016/j.jsb.2013.07.005 · DOI
- Maeshima, 2008, Packaging the genome: the structure of mitotic chromosomes, J. Biochem., 143, 145, 10.1093/jb/mvm214 · DOI
- Maresca, 2005, Histone H1 is essential for mitotic chromosome architecture and segregation in Xenopus laevis egg extracts, J. Cell Biol., 169, 859, 10.1083/jcb.200503031 · DOI
- Marrero, 2012, The crystal structure of human α2-macroglobulin reveals a unique molecular cage, Angew. Chem. Int. Ed. Engl., 51, 3340, 10.1002/anie.201108015 · DOI
- McGinty, 2015, Nucleosome structure and function, Chem. Rev., 115, 2255, 10.1021/cr500373h · DOI · Paper page
- Murray, 1991, Cell cycle extracts, Methods Cell Biol., 36, 581, 10.1016/S0091-679X(08)60298-8 · DOI
- Nakane, 2020, Single-particle cryo-EM at atomic resolution, Nature, 587, 152, 10.1038/s41586-020-2829-0 · DOI
- Nguyen, 2019, Structure of an endosomal signaling GPCR-G protein-β-arrestin megacomplex, Nat. Struct. Mol. Biol., 26, 1123, 10.1038/s41594-019-0330-y · DOI
- Nishino, 2012, Human mitotic chromosomes consist predominantly of irregularly folded nucleosome fibres without a 30-nm chromatin structure, EMBO J., 31, 1644, 10.1038/emboj.2012.35 · DOI
- Ohno, 2019, Sub-nucleosomal Genome Structure Reveals Distinct Nucleosome Folding Motifs, Cell, 176, 520, 10.1016/j.cell.2018.12.014 · DOI
- Olins, 2003, Chromatin history: our view from the bridge, Nat. Rev. Mol. Cell Biol., 4, 809, 10.1038/nrm1225 · DOI
- Pettersen, 2004, UCSF Chimera--a visualization system for exploratory research and analysis, J. Comput. Chem., 25, 1605, 10.1002/jcc.20084 · DOI
- Piovesan, 2016, The RING 2.0 web server for high quality residue interaction networks, Nucleic Acids Res., 44, W367, 10.1093/nar/gkw315 · DOI
- Punjani, 2021, 3D variability analysis: resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM, J. Struct. Biol., 213, 107702, 10.1016/j.jsb.2021.107702 · DOI
- Punjani, 2017, cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination, Nat. Methods, 14, 290, 10.1038/nmeth.4169 · DOI · Paper page
- Renz, 1977, Involvement of histone H1 in the organization of the chromosome fiber, Proc. Natl. Acad. Sci. USA, 74, 1879, 10.1073/pnas.74.5.1879 · DOI
- Ricci, 2015, Chromatin fibers are formed by heterogeneous groups of nucleosomes in vivo, Cell, 160, 1145, 10.1016/j.cell.2015.01.054 · DOI · Paper page
- Richmond, 1984, Structure of the nucleosome core particle at 7 A resolution, Nature, 311, 532, 10.1038/311532a0 · DOI
- Risca, 2017, Variable chromatin structure revealed by in situ spatially correlated DNA cleavage mapping, Nature, 541, 237, 10.1038/nature20781 · DOI
- Robinson, 2006, EM measurements define the dimensions of the “30-nm” chromatin fiber: evidence for a compact, interdigitated structure, Proc. Natl. Acad. Sci. USA, 103, 6506, 10.1073/pnas.0601212103 · DOI
- Samejima, 2018, Functional analysis after rapid degradation of condensins and 3D-EM reveals chromatin volume is uncoupled from chromosome architecture in mitosis, J. Cell Sci., 131, jcs210187, 10.1242/jcs.210187 · DOI
- Sanulli, 2019, HP1 reshapes nucleosome core to promote phase separation of heterochromatin, Nature, 575, 390, 10.1038/s41586-019-1669-2 · DOI
- Schalch, 2005, X-ray structure of a tetranucleosome and its implications for the chromatin fibre, Nature, 436, 138, 10.1038/nature03686 · DOI
- Scheffer, 2011, Evidence for short-range helical order in the 30-nm chromatin fibers of erythrocyte nuclei, Proc. Natl. Acad. Sci. USA, 108, 16992, 10.1073/pnas.1108268108 · DOI
- Scheres, 2012, RELION: implementation of a Bayesian approach to cryo-EM structure determination, J. Struct. Biol., 180, 519, 10.1016/j.jsb.2012.09.006 · DOI · Paper page
- Scheres, 2007, Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization, Nat. Methods, 4, 27, 10.1038/nmeth992 · DOI
- Schneider, 2012, NIH Image to ImageJ: 25 years of image analysis, Nat. Methods, 9, 671, 10.1038/nmeth.2089 · DOI · Paper page
- Shamu, 1992, Sister chromatid separation in frog egg extracts requires DNA topoisomerase II activity during anaphase, J. Cell Biol., 117, 921, 10.1083/jcb.117.5.921 · DOI
- Shechter, 2009, A distinct H2A.X isoform is enriched in Xenopus laevis eggs and early embryos and is phosphorylated in the absence of a checkpoint, Proc. Natl. Acad. Sci. USA, 106, 749, 10.1073/pnas.0812207106 · DOI
- Shevchenko, 2006, In-gel digestion for mass spectrometric characterization of proteins and proteomes, Nat. Protoc., 1, 2856, 10.1038/nprot.2006.468 · DOI
- Sinha, 2017, Distortion of histone octamer core promotes nucleosome mobilization by a chromatin remodeler, Science, 355, eaaa3761, 10.1126/science.aaa3761 · DOI
- Skrajna, 2020, Comprehensive nucleosome interactome screen establishes fundamental principles of nucleosome binding, Nucleic Acids Res., 48, 9415, 10.1093/nar/gkaa544 · DOI
- Song, 2014, Cryo-EM study of the chromatin fiber reveals a double helix twisted by tetranucleosomal units, Science, 344, 376, 10.1126/science.1251413 · DOI
- Su, 2021, A ‘Build and Retrieve’ methodology to simultaneously solve cryo-EM structures of membrane proteins, Nat. Methods, 18, 69, 10.1038/s41592-020-01021-2 · DOI
- Takahashi, 2019, Folding the genome into mitotic chromosomes, Curr. Opin. Cell Biol., 60, 19, 10.1016/j.ceb.2019.03.005 · DOI
- Tan, 2021, Heterogeneous non-canonical nucleosomes predominate in yeast cells in situ, bioRxiv
- Turner, 2018, Highly disordered histone H1-DNA model complexes and their condensates, Proc. Natl. Acad. Sci. USA, 115, 11964, 10.1073/pnas.1805943115 · DOI
- Vargas, 2014, Efficient initial volume determination from electron microscopy images of single particles, Bioinformatics, 30, 2891, 10.1093/bioinformatics/btu404 · DOI
- Verbeke, 2018, Classification of Single Particles from Human Cell Extract Reveals Distinct Structures, Cell Rep., 24, 259, 10.1016/j.celrep.2018.06.022 · DOI
- Verbeke, 2020, Separating distinct structures of multiple macromolecular assemblies from cryo-EM projections, J. Struct. Biol., 209, 107416, 10.1016/j.jsb.2019.107416 · DOI
- Wang, 2013, Histone modifications and mitosis: countermarks, landmarks, and bookmarks, Trends Cell Biol., 23, 175, 10.1016/j.tcb.2012.11.005 · DOI
- Wangkanont, 2016, Structures of Xenopus embryonic epidermal lectin reveal a conserved mechanism of microbial glycan recognition, J. Biol. Chem., 291, 5596, 10.1074/jbc.M115.709212 · DOI
- Waterhouse, 2018, SWISS-MODEL: homology modelling of protein structures and complexes, Nucleic Acids Res., 46, W296, 10.1093/nar/gky427 · DOI
- Weber, 2014, Nucleosomes are context-specific, H2A.Z-modulated barriers to RNA polymerase, Mol. Cell, 53, 819, 10.1016/j.molcel.2014.02.014 · DOI
- Willcockson, 2021, H1 histones control the epigenetic landscape by local chromatin compaction, Nature, 589, 293, 10.1038/s41586-020-3032-z · DOI
- Willhoft, 2018, Structure and dynamics of the yeast SWR1-nucleosome complex, Science, 362, eaat7716, 10.1126/science.aat7716 · DOI
- Woods, 2020, Elucidating the influence of linker histone variants on chromatosome dynamics and energetics, Nucleic Acids Res., 48, 3591, 10.1093/nar/gkaa121 · DOI
- Wühr, 2014, Deep proteomics of the Xenopus laevis egg using an mRNA-derived reference database, Curr. Biol., 24, 1467, 10.1016/j.cub.2014.05.044 · DOI
- Yan, 2019, Structures of the ISWI-nucleosome complex reveal a conserved mechanism of chromatin remodeling, Nat. Struct. Mol. Biol., 26, 258, 10.1038/s41594-019-0199-9 · DOI
- Ye, 2019, Structure of the RSC complex bound to the nucleosome, Science, 366, 838, 10.1126/science.aay0033 · DOI
- Yi, 2019, Electron microscopy snapshots of single particles from single cells, J. Biol. Chem., 294, 1602, 10.1074/jbc.RA118.006686 · DOI
- Yusufova, 2021, Histone H1 loss drives lymphoma by disrupting 3D chromatin architecture, Nature, 589, 299, 10.1038/s41586-020-3017-y · DOI
- Zheng, 2017, MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy, Nat. Methods, 14, 331, 10.1038/nmeth.4193 · DOI
- Zhiteneva, 2017, Mitotic post-translational modifications of histones promote chromatin compaction in vitro, Open Biol., 7, 170076, 10.1098/rsob.170076 · DOI
- Zhou, 2015, Structural Mechanisms of Nucleosome Recognition by Linker Histones, Mol. Cell, 59, 628, 10.1016/j.molcel.2015.06.025 · DOI
- Zhou, 2019, Atomic resolution cryo-EM structure of a native-like CENP-A nucleosome aided by an antibody fragment, Nat. Commun., 10, 2301, 10.1038/s41467-019-10247-4 · DOI
- Zhou, 2021, Structural basis of nucleosome dynamics modulation by histone variants H2A.B and H2A.Z.2.2, EMBO J., 40, e105907, 10.15252/embj.2020105907 · DOI
- Zierhut, 2014, Nucleosomal regulation of chromatin composition and nuclear assembly revealed by histone depletion, Nat. Struct. Mol. Biol., 21, 617, 10.1038/nsmb.2845 · DOI
- Zlatanova, 2009, The nucleosome family: dynamic and growing, Structure, 17, 160, 10.1016/j.str.2008.12.016 · DOI
- Zou, 2018, Direct Observation of H3-H4 Octasome by High-Speed AFM, Chemistry, 24, 15998, 10.1002/chem.201804010 · DOI
Metadata
- Authors
- Arimura, Y., Shih, R. M., Froom, R., & Funabiki, H.
- Affiliations
- Rockefeller University (US)
- Corresponding author
- Arimura, Yasuhiro
- Funabiki, Hironori
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2021-11
- Volume
- 81
- Issue
- 21
- Pages
- 4377-4397.e12
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC8571072
- OpenAlex
- W3196371936
- Cited by
- 59
- References
- 2
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 9 · 2023: 7 · 2022: 12 · 2021: 3
- FWCI
- 2.43
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 368 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Japan Society for the Promotion of Science
- National Institutes of Health (R35GM132111)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- nucleosome structure, interphase chromosomes, metaphase chromosomes, chromatin structure, linker DNA, chromatosome, DNA supercoiling, cell cycle, post-translational modification, cryo-EM structure determination
- MeSH terms
- Protein Domains, Animals, Cell Communication, Cell Cycle, Cell Division, Chromatin, Chromosomes, Computer Simulation, DNA, Humans, Interphase, Metaphase, Nucleosomes, Protein Conformation, Protein Processing, Post-Translational, Xenopus, Cryoelectron Microscopy, Hydrophobic and Hydrophilic Interactions
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