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4 results on '"MESH: Histone Chaperones"'

1. Histone variant H2A.Z regulates zygotic genome activation

Author

Alejandro Gomez-Auli, Nicola Iovino, Michael Rauer, Dafne Ibarra-Morales, Mariana Schulte-Sasse, Francesco Cardamone, Leily Rabbani, Piergiuseppe Quarato, Fides Zenk, Germano Cecere, Max Planck Institute of Immunobiology and Epigenetics (MPI-IE), Max-Planck-Gesellschaft, Mécanismes de l'Hérédité épigénétique / Mechanisms of epigenetic inheritance, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Open Access funding enabled and organized by Projekt DEAL, and Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)

Subjects
Epigenomics, Male, Zygote, MESH: Drosophila, [SDV]Life Sciences [q-bio], MESH: Epigenomics, General Physics and Astronomy, RNA polymerase II, Genome, MESH: Down-Regulation, Histones, 0302 clinical medicine, MESH: Gene Expression Regulation, Developmental, MESH: Embryonic Development, MESH: Animals, Histone variants, Adenosine Triphosphatases, MESH: Histones, 0303 health sciences, Genes, Essential, Multidisciplinary, biology, MESH: Histone Chaperones, Gene Expression Regulation, Developmental, Chromatin, Cell biology, Housekeeping gene, Histone, Gene Knockdown Techniques, Chromatin Immunoprecipitation Sequencing, MESH: Cell Division, Drosophila, Female, RNA Polymerase II, MESH: Transcription Initiation Site, Transcription Initiation Site, MESH: Chromatin Immunoprecipitation Sequencing, Cell Division, Transcriptional Activation, Epigenetic memory, animal structures, Science, Down-Regulation, Embryonic Development, Article, General Biochemistry, Genetics and Molecular Biology, MESH: Chromatin, 03 medical and health sciences, MESH: Adenosine Triphosphatases, Animals, Histone Chaperones, MESH: Genome, Gene, MESH: Genes, Essential, 030304 developmental biology, Pioneer factor, General Chemistry, MESH: Gene Knockdown Techniques, MESH: Male, MESH: RNA Polymerase II, biology.protein, MESH: Transcriptional Activation, Maternal to zygotic transition, MESH: Zygote, MESH: Female, 030217 neurology & neurosurgery
Abstract

During embryogenesis, the genome shifts from transcriptionally quiescent to extensively active in a process known as Zygotic Genome Activation (ZGA). In Drosophila, the pioneer factor Zelda is known to be essential for the progression of development; still, it regulates the activation of only a small subset of genes at ZGA. However, thousands of genes do not require Zelda, suggesting that other mechanisms exist. By conducting GRO-seq, HiC and ChIP-seq in Drosophila embryos, we demonstrate that up to 65% of zygotically activated genes are enriched for the histone variant H2A.Z. H2A.Z enrichment precedes ZGA and RNA Polymerase II loading onto chromatin. In vivo knockdown of maternally contributed Domino, a histone chaperone and ATPase, reduces H2A.Z deposition at transcription start sites, causes global downregulation of housekeeping genes at ZGA, and compromises the establishment of the 3D chromatin structure. We infer that H2A.Z is essential for the de novo establishment of transcriptional programs during ZGA via chromatin reorganization., Nature Communications, 12 (1), ISSN:2041-1723

Published
2021
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2. Modulation of chromatin structure by the FACT histone chaperone complex regulates HIV-1 integration

Author

Matysiak, Julien, Lesbats, Paul, Mauro, Eric, Lapaillerie, Delphine, Dupuy, Jean-William, Lopez, Angelica P., Benleulmi, Mohamed Salah, Calmels, Christina, Andreola, Marie-Line, Ruff, Marc, Llano, Manuel, Delelis, Olivier, Lavigne, Marc, Parissi, Vincent, Microbiologie Fondamentale et Pathogénicité (MFP), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Centre Génomique Fonctionnelle Bordeaux [Bordeaux] (CGFB), Institut Polytechnique de Bordeaux-Université de Bordeaux Ségalen [Bordeaux 2], University of Texas [El Paso] (UTEP ), Institut de génétique et biologie moléculaire et cellulaire (IGBMC), Université Louis Pasteur - Strasbourg I-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), École normale supérieure - Cachan (ENS Cachan)-Centre National de la Recherche Scientifique (CNRS), Virologie (CNRS - UMR3569), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), This work was supported by the French National Research Agency (ANR, RETROSelect, jcjc2011 program), the French National Research Agency against AIDS (ANRS, AO2016), SIDACTION (AO2016, VIH20160721002), the French Infrastructure for Integrated Structural Biology (FRISBI) ANR-10-INSB-05-01, Instruct, a part of the European Strategy Forum on Research Infrastructures (ESFRI), the Centre National de la Recherche Scientifique (CNRS), the University of Bordeaux., ANR-11-JSV3-0006,RetroSelect,Contrôle cellulaire de la sélectivité de l'intégration rétrovirale(2011), ANR-10-INBS-0005,FRISBI,Infrastructure Française pour la Biologie Structurale Intégrée(2010), ruff, marc, Jeunes Chercheuses et Jeunes Chercheurs - Contrôle cellulaire de la sélectivité de l'intégration rétrovirale - - RetroSelect2011 - ANR-11-JSV3-0006 - JCJC - VALID, and Infrastructure Française pour la Biologie Structurale Intégrée - - FRISBI2010 - ANR-10-INBS-0005 - INBS - VALID

Subjects
lcsh:Immunologic diseases. Allergy, Virus Integration, FACT, Retroviral integration, HIV Infections, HIV Integrase, Integrase, MESH: Chromatin, MESH: HIV-1, MESH: Nucleosomes, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Humans, MESH: Protein Binding, Histone Chaperones, MESH: Intercellular Signaling Peptides and Proteins, Cells, Cultured, [SDV.MP.VIR] Life Sciences [q-bio]/Microbiology and Parasitology/Virology, MESH: Humans, Research, MESH: Host-Pathogen Interactions, MESH: Chromatin Assembly and Disassembly, MESH: Histone Chaperones, MESH: HIV Infections, Chromatin Assembly and Disassembly, Chromatin, Nucleosomes, Nucleosome, Host-Pathogen Interactions, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases, HIV-1, Intercellular Signaling Peptides and Proteins, MESH: HIV Integrase, lcsh:RC581-607, MESH: Virus Integration, Protein Binding, MESH: Cells, Cultured
Abstract

Background Insertion of retroviral genome DNA occurs in the chromatin of the host cell. This step is modulated by chromatin structure as nucleosomes compaction was shown to prevent HIV-1 integration and chromatin remodeling has been reported to affect integration efficiency. LEDGF/p75-mediated targeting of the integration complex toward RNA polymerase II (polII) transcribed regions ensures optimal access to dynamic regions that are suitable for integration. Consequently, we have investigated the involvement of polII-associated factors in the regulation of HIV-1 integration. Results Using a pull down approach coupled with mass spectrometry, we have selected the FACT (FAcilitates Chromatin Transcription) complex as a new potential cofactor of HIV-1 integration. FACT is a histone chaperone complex associated with the polII transcription machinery and recently shown to bind LEDGF/p75. We report here that a tripartite complex can be formed between HIV-1 integrase, LEDGF/p75 and FACT in vitro and in cells. Biochemical analyzes show that FACT-dependent nucleosome disassembly promotes HIV-1 integration into chromatinized templates, and generates highly favored nucleosomal structures in vitro. This effect was found to be amplified by LEDGF/p75. Promotion of this FACT-mediated chromatin remodeling in cells both increases chromatin accessibility and stimulates HIV-1 infectivity and integration. Conclusions Altogether, our data indicate that FACT regulates HIV-1 integration by inducing local nucleosomes dissociation that modulates the functional association between the incoming intasome and the targeted nucleosome. Electronic supplementary material The online version of this article (doi:10.1186/s12977-017-0363-4) contains supplementary material, which is available to authorized users.

Published
2017
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3. Regulation of ALT-associated homology-directed repair by polyADP-ribosylation

Author

Ian D. Waddell, Robert W. Sobol, Kate M. Smith, Justin L. Roncaioli, Felipe da Veiga Leprevost, Song My Hoang, Dattatreya Mellacharevu, Dominique Ray-Gallet, Michelle L. Lynskey, Roderick J. O’Sullivan, Ragini Bhargava, Jonathan Barroso-González, Nicole Kaminski, Geneviève Almouzni, Anne R. Wondisford, Jianfeng Li, Donald J. Ogilvie, Alexey I. Nesvizhskii, Dominic I. James, Callen T. Wallace, Simon C. Watkins, Laura García-Expósito, University of Pittsburgh School of Medicine, Pennsylvania Commonwealth System of Higher Education (PCSHE), University of Manchester [Manchester], University of Michigan [Ann Arbor], University of Michigan System, University of South Alabama, Dynamique du noyau [Institut Curie], Institut Curie [Paris]-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), and HAL-SU, Gestionnaire

Subjects
MESH: Signal Transduction, Poly Adenosine Diphosphate Ribose, Cell Cycle Proteins, Histones, Poly ADP Ribosylation, 0302 clinical medicine, Structural Biology, MESH: RNA, Small Interfering, RNA, Small Interfering, MESH: Histones, 0303 health sciences, PARG, MESH: X-linked Nuclear Protein, biology, MESH: Histone Chaperones, DNA, Neoplasm, MESH: Transcription Factors, MESH: Gene Expression Regulation, Neoplastic, Telomere, Chromatin, Cell biology, Gene Expression Regulation, Neoplastic, MESH: Recombinational DNA Repair, Histone, MESH: Poly Adenosine Diphosphate Ribose, MESH: Epithelial Cells, [SDV.BBM.GTP] Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], Poly(ADP-ribose) Polymerases, Signal Transduction, G2 Phase, X-linked Nuclear Protein, MESH: Cell Line, Tumor, Glycoside Hydrolases, DNA repair, DNA damage, MESH: DNA, Neoplasm, Article, MESH: Chromatin, MESH: Telomere Homeostasis, Homology directed repair, 03 medical and health sciences, MESH: Cell Cycle Proteins, Cell Line, Tumor, [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Genomics [q-bio.GN], MESH: Glycoside Hydrolases, Humans, Histone Chaperones, Molecular Biology, ATRX, 030304 developmental biology, MESH: DNA Damage, MESH: Humans, MESH: Poly ADP Ribosylation, MESH: Poly(ADP-ribose) Polymerases, Recombinational DNA Repair, Telomere Homeostasis, Epithelial Cells, MESH: G2 Phase, MESH: Protein Processing, Post-Translational, MESH: HeLa Cells, biology.protein, MESH: Telomere, Protein Processing, Post-Translational, 030217 neurology & neurosurgery, DNA Damage, HeLa Cells, Transcription Factors
Abstract

International audience; The synthesis of poly(ADP-ribose) (PAR) reconfigures the local chromatin environment and recruits DNA-repair complexes to damaged chromatin. PAR degradation by poly(ADP-ribose) glycohydrolase (PARG) is essential for progression and completion of DNA repair. Here, we show that inhibition of PARG disrupts homology-directed repair (HDR) mechanisms that underpin alternative lengthening of telomeres (ALT). Proteomic analyses uncover a new role for poly(ADP-ribosyl)ation (PARylation) in regulating the chromatin-assembly factor HIRA in ALT cancer cells. We show that HIRA is enriched at telomeres during the G2 phase and is required for histone H3.3 deposition and telomere DNA synthesis. Depletion of HIRA elicits systemic death of ALT cancer cells that is mitigated by re-expression of ATRX, a protein that is frequently inactivated in ALT tumors. We propose that PARylation enables HIRA to fulfill its essential role in the adaptive response to ATRX deficiency that pervades ALT cancers.

Published
2020
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4. Dynamics of Histone H3 Deposition In Vivo Reveal a Nucleosome Gap-Filling Mechanism for H3.3 to Maintain Chromatin Integrity

Author

Lars E.T. Jansen, Isabelle Vassias, Céline Pellentz, Peter D. Adams, David C. Schultz, Dominique Ray-Gallet, Geneviève Almouzni, Nikolay A. Pchelintsev, Adam Woolfe, Nicolas Lacoste, Aastha Puri, Dynamique nucléaire et plasticité du génome (DNPG), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Neurobiologie des Réseaux Sensorimoteurs (LNRS), Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5), Laboratoire du Métabolisme de l'ADN et Réponses aux Génotoxiques (LMARG), Département Biologie des Génomes (DBG), Institut de Biologie Intégrative de la Cellule (I2BC), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Institut de Biologie Intégrative de la Cellule (I2BC), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Saclay, The Wistar Institute, Protein Production, Libraries & Molecular Screening Facility, The Beatson Institute for Cancer Research, Epigenetics of Cancer and Ageing, Instituto Gulbenkian de Ciência [Oeiras] (IGC), Fundação Calouste Gulbenkian, European Project: 249994,EC:FP7:ERC,ERC-2009-AdG,ECCENTRIC(2010), Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut Curie [Paris]-Centre National de la Recherche Scientifique (CNRS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), and University of Glasgow

Subjects
DNA Replication, RNA polymerase II, MESH: DNA Replication, Cell Cycle Proteins, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Histones, 03 medical and health sciences, chemistry.chemical_compound, Histone H3, 0302 clinical medicine, MESH: Cell Cycle Proteins, Transcription (biology), MESH: Nucleosomes, Nucleosome, Humans, Histone Chaperones, Molecular Biology, 030304 developmental biology, Genetics, MESH: Histones, 0303 health sciences, MESH: Humans, Deoxyribonucleases, biology, DNA replication, MESH: Histone Chaperones, Cell Biology, MESH: Transcription Factors, Cell biology, Chromatin, MESH: RNA Polymerase II, Nucleosomes, Chromatin Assembly Factor-1, chemistry, Naked DNA, MESH: HeLa Cells, biology.protein, RNA Polymerase II, MESH: Molecular Chaperones, 030217 neurology & neurosurgery, DNA, MESH: Chromatin Assembly Factor-1, MESH: Deoxyribonucleases, HeLa Cells, Molecular Chaperones, Transcription Factors
Abstract

The deposited article is a post-print version and has peer review. The deposited article version contains attached the supplementary materials within the pdf. This publication hasn't any creative commons license associated. Establishment of a proper chromatin landscape is central to genome function. Here, we explain H3 variant distribution by specific targeting and dynamics of deposition involving the CAF-1 and HIRA histone chaperones. Impairing replicative H3.1 incorporation via CAF-1 enables an alternative H3.3 deposition at replication sites via HIRA. Conversely, the H3.3 incorporation throughout the cell cycle via HIRA cannot be replaced by H3.1. ChIP-seq analyses reveal correlation between HIRA-dependent H3.3 accumulation and RNA pol II at transcription sites and specific regulatory elements, further supported by their biochemical association. The HIRA complex shows unique DNA binding properties, and depletion of HIRA increases DNA sensitivity to nucleases. We propose that protective nucleosome gap filling of naked DNA by HIRA leads to a broad distribution of H3.3, and HIRA association with Pol II ensures local H3.3 enrichment at specific sites. We discuss the importance of this H3.3 deposition as a salvage pathway to maintain chromatin integrity. Ligue Nationale contre le Cancer (Equipe labellisée Ligue 2010); PIC Programs; the European Commission Network of Excellence EpiGeneSys (HEALTH-F4-2010-257082), the European Commission ITN FP7-PEOPLE-2007-215148 “Image DDR” and FP7-PEOPLE-2008-238176 “Nucleosome 4D,” ERC Advanced Grant 2009-AdG_20090506 “Eccentric,” the European Commission large-scale integrating project FP7_HEALTH-2010-259743 “MODHEP,” ANR “ECenS” ANR-09-BLAN-0257-01, ANR “ChromaTin” ANR-10-BLAN-1326-03, and INCa “GepiG.” The lab of P.D.A. is funded by NIA program project P01 AG031862. L.E.T.J. was supported by the Fundação Calouste Gulbenkian, Fundação para a Ciência e a Tecnologia (FCT) grant BIA-PRO/100537/2008, the European Commission FP7 programme, and an EMBO installation grant. info:eu-repo/semantics/publishedVersion

Published
2011
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