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8 results on '"MESH : Chromatin"'

1. Trm112p Is a 15-kDa Zinc Finger Protein Essential for the Activity of Two tRNA and One Protein Methyltransferases in Yeast

Author

Léon Dirick, Bruno Lapeyre, Glenn R. Björk, Marie-Hélène Mazauric, Suresh K. Purushothaman, Centre de recherches de biochimie macromoléculaire ( CRBM ), Université Montpellier 1 ( UM1 ) -Université Montpellier 2 - Sciences et Techniques ( UM2 ) -IFR122-Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Centre de recherche en Biologie Cellulaire (CRBM), Université Montpellier 2 - Sciences et Techniques (UM2)-Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 1 (UM1), Institut de Génétique Moléculaire de Montpellier (IGMM), and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)

Subjects
Proteomics, MESH : DNA, MESH: tRNA Methyltransferases, MESH : Saccharomyces cerevisiae, MESH : Models, Genetic, Biochemistry, MESH: Recombinant Proteins, MESH : Proteomics, MESH: Saccharomyces cerevisiae Proteins, MESH : Anticodon, RNA, Transfer, MESH : Catalysis, MESH: Models, Genetic, Zinc finger, tRNA Methyltransferases, MESH : Cell Nucleus, 0303 health sciences, MESH : Chromatin, MESH: Proteomics, 030302 biochemistry & molecular biology, MESH: DNA, Zinc Fingers, MESH : Protein Binding, Translation (biology), MESH: Saccharomyces cerevisiae, MESH : Mitosis, Chromatin, Recombinant Proteins, MESH : tRNA Methyltransferases, Transfer RNA, T arm, MESH : Mutation, Protein Binding, MESH: Cell Nucleus, TRNA modification, Saccharomyces cerevisiae Proteins, MESH: Mutation, MESH : Recombinant Proteins, Saccharomyces cerevisiae, Mitosis, MESH : RNA, Transfer, Biology, Catalysis, Chromatin remodeling, MESH: Chromatin, MESH : Saccharomyces cerevisiae Proteins, 03 medical and health sciences, Anticodon, MESH: Anticodon, MESH: Zinc Fingers, MESH: Protein Binding, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Zinc Fingers, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, Molecular Biology, 030304 developmental biology, Cell Nucleus, Models, Genetic, TRNA Methyltransferase, DNA, Cell Biology, MESH: Mitosis, MESH: Catalysis, MESH: RNA, Transfer, biology.organism_classification, Mutation, RNA
Abstract

International audience; The degenerate base at position 34 of the tRNA anticodon is the target of numerous modification enzymes. In Saccharomyces cerevisiae, five tRNAs exhibit a complex modification of uridine 34 (mcm(5)U(34) and mcm(5)s(2)U(34)), the formation of which requires at least 25 different proteins. The addition of the last methyl group is catalyzed by the methyltransferase Trm9p. Trm9p interacts with Trm112p, a 15-kDa protein with a zinc finger domain. Trm112p is essential for the activity of Trm11p, another tRNA methyltransferase, and for Mtq2p, an enzyme that methylates the translation termination factor eRF1/Sup45. Here, we report that Trm112p is required in vivo for the formation of mcm(5)U(34) and mcm(5)s(2)U(34). When produced in Escherichia coli, Trm112p forms a complex with Trm9p, which renders the latter soluble. This recombinant complex catalyzes the formation of mcm(5)U(34) on tRNA in vitro but not mcm(5)s(2)U(34). An mtq2-0 trm9-0 strain exhibits a synthetic growth defect, thus revealing the existence of an unexpected link between tRNA anticodon modification and termination of translation. Trm112p is associated with other partners involved in ribosome biogenesis and chromatin remodeling, suggesting that it has additional roles in the cell.

Published
2010

2. A vlincRNA participates in senescence maintenance by relieving H2AZ-mediated repression at the INK4 locus

Author

Lazorthes, Sandra, Vallot, Céline, Briois, Sébastien, Aguirrebengoa, Marion, Thuret, Jean-Yves, St Laurent, Georges, Rougeulle, Claire, Kapranov, Philipp, Mann, Carl, Trouche, Didier, Nicolas, Estelle, Laboratoire de Biologie Cellulaire et Moléculaire du Contrôle de la Prolifération (LBCMCP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre épigénétique et destin cellulaire (EDC (UMR_7216)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Institut de Biologie et de Technologies de Saclay (IBITECS), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Sénescence et stabilité génomique (SEN), 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)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-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), Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Université Paris-Sud - Paris 11 (UP11)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), St Laurent Institute, St. Laurent Institute, Institute of Genomics, Huaqiao University School of Medicine, Xiamen, Academy of Biology and Biotechnology, Southern Federal University [Rostov-on-Don] (SFEDU), LBCMCP, Centre National de la Recherche Scientifique ( CNRS ), Centre épigénétique et destin cellulaire ( EDC ), Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Biologie et de Technologies de Saclay ( IBITECS ), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), Sénescence et stabilité génomique ( SEN ), 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 ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -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 ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Woburn, Massachusetts, Southern Federal University - Rostov on Don, Université de Toulouse (UT)-Université de Toulouse (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), Université de Toulouse (UT)-Université de Toulouse (UT)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Centre épigénétique et destin cellulaire (EDC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, 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), Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Centre de Biologie Intégrative (CBI), and Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)

Subjects
MESH : Cell Line, RNA, Untranslated, MESH : RNA, Untranslated, MESH: Humans, MESH : Chromatin, [ SDV ] Life Sciences [q-bio], MESH : Cell Aging, MESH : Heterochromatin, [SDV]Life Sciences [q-bio], MESH : Humans, Chromatin, Article, Cell Line, MESH: Cell Line, MESH: Chromatin, MESH: RNA, Untranslated, MESH: Heterochromatin, MESH: Cell Aging, Heterochromatin, Humans, Erratum, ComputingMilieux_MISCELLANEOUS, Cellular Senescence
Abstract

Non-coding RNAs (ncRNAs) play major roles in proper chromatin organization and function. Senescence, a strong anti-proliferative process and a major anticancer barrier, is associated with dramatic chromatin reorganization in heterochromatin foci. Here we analyze strand-specific transcriptome changes during oncogene-induced human senescence. Strikingly, while differentially expressed RNAs are mostly repressed during senescence, ncRNAs belonging to the recently described vlincRNA (very long intergenic ncRNA) class are mainly activated. We show that VAD, a novel antisense vlincRNA strongly induced during senescence, is required for the maintenance of senescence features. VAD modulates chromatin structure in cis and activates gene expression in trans at the INK4 locus, which encodes cell cycle inhibitors important for senescence-associated cell proliferation arrest. Importantly, VAD inhibits the incorporation of the repressive histone variant H2A.Z at INK4 gene promoters in senescent cells. Our data underline the importance of vlincRNAs as sensors of cellular environment changes and as mediators of the correct transcriptional response., Senescence is associated with chromatin reorganization in heterochromatin foci. Here the authors show that VAD, a very long intergenic non-coding RNA activated by senescence, inhibits the incorporation of the repressive histone variant H2A.Z to INK4 promoters in senescent cells.

Published
2015

3. Live-Cell Imaging Reveals Multiple Interactions between Epstein-Barr Virus Nuclear Antigen 1 and Cellular Chromatin during Interphase and Mitosis

Author

Maïté Coppey-Moisan, Tristan Piolot, Vincent Maréchal, Gabriel Dos Reis, Christophe Klein, Nathalie Jourdan, Marc Tramier, Frédérique Quignon, Aude Jobart-Malfait, Adaptation Biologique et Vieillissement = Biological Adaptation and Ageing (B2A), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Paris Seine (IBPS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut Jacques Monod (IJM (UMR_7592)), Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherche des Cordeliers (CRC (UMR_S 872)), Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Centre de Recherche des Cordeliers ( CRC (UMR_S 872) ), Université Pierre et Marie Curie - Paris 6 ( UPMC ) -Université Paris Descartes - Paris 5 ( UPD5 ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut Jacques Monod ( IJM ), Université Paris Diderot - Paris 7 ( UPD7 ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique et Développement de Rennes ( IGDR ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Centre National de la Recherche Scientifique ( CNRS ) -Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), UPMC, INSERM, Université Paris Descartes - Paris 5 (UPD5)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), and De Villemeur, Hervé

Subjects
MESH : Cell Line, viruses, [SDV]Life Sciences [q-bio], Gene Expression, MESH : Hepatocytes, MESH: Hepatocytes, Chromatin bridge, 0302 clinical medicine, MESH : Protein Transport, hemic and lymphatic diseases, MESH : Protein Stability, 0303 health sciences, MESH : Chromatin, MESH : Epstein-Barr Virus Nuclear Antigens, MESH : Interphase, Protein Stability, RNA-Binding Proteins, MESH : Protein Binding, Cell cycle, MESH : Mitosis, Chromatin, Virus-Cell Interactions, Protein Transport, 030220 oncology & carcinogenesis, Premature chromosome condensation, Interphase, MESH: Cell Nucleolus, MESH : Carrier Proteins, MESH: Epstein-Barr Virus Nuclear Antigens, Cell Nucleolus, Plasmids, Protein Binding, MESH: Protein Transport, MESH: Gene Expression, Immunology, Mitosis, MESH: Carrier Proteins, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Microbiology, Cell Line, MESH: Chromatin, MESH: Interphase, 03 medical and health sciences, G2 phase, Prophase, MESH: Plasmids, MESH: Protein Stability, Virology, MESH: HMGB2 Protein, HMGB2 Protein, Humans, MESH: Protein Binding, [SDV.BC] Life Sciences [q-bio]/Cellular Biology, 030304 developmental biology, MESH: Humans, [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology, MESH : Humans, MESH: Mitosis, MESH : HMGB2 Protein, Molecular biology, MESH: Cell Line, MESH : Gene Expression, Epstein-Barr Virus Nuclear Antigens, MESH : Plasmids, Insect Science, MESH : Cell Nucleolus, Hepatocytes, Carrier Proteins
Abstract

Epstein-Barr virus (EBV) establishes a life-long latent infection in humans. In proliferating latently infected cells, EBV genomes persist as multiple episomes that undergo one DNA replication event per cell cycle and remain attached to the mitotic chromosomes. EBV nuclear antigen 1 (EBNA-1) binding to the episome and cellular genome is essential to ensure proper episome replication and segregation. However, the nature and regulation of EBNA-1 interaction with chromatin has not been clearly elucidated. This activity has been suggested to involve EBNA-1 binding to DNA, duplex RNA, and/or proteins. EBNA-1 binding protein 2 (EBP2), a nucleolar protein, has been proposed to act as a docking protein for EBNA-1 on mitotic chromosomes. However, there is no direct evidence thus far for EBP2 being associated with EBNA-1 during mitosis. By combining video microscopy and Förster resonance energy transfer (FRET) microscopy, we demonstrate here for the first time that EBNA-1 and EBP2 interact in the nucleoplasm, as well as in the nucleoli during interphase. However, in strong contrast to the current proposed model, we were unable to observe any interaction between EBNA-1 and EBP2 on mitotic chromosomes. We also performed a yeast double-hybrid screening, followed by a FRET analysis, that led us to identify HMGB2 (high-mobility group box 2), a well-known chromatin component, as a new partner for EBNA-1 on chromatin during interphase and mitosis. Although the depletion of HMGB2 partly altered EBNA-1 association with chromatin in HeLa cells during interphase and mitosis, it did not significantly impact the maintenance of EBV episomes in Raji cells.

Published
2012

4. A mono-allelic bivalent chromatin domain controls tissue-specific imprinting at Grb10

Author

Stormy J. Chamberlain, Jean-Philippe Hugnot, Terry Magnuson, Robert Feil, Lionel A. Sanz, Jean Charles Sabourin, Amandine Henckel, Philippe Arnaud, Institut de Génétique Moléculaire de Montpellier (IGMM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Department of Genetics, University of North Carolina [Chapel Hill] (UNC), University of North Carolina System (UNC)-University of North Carolina System (UNC)-Carolina Center for the Genome Sciences, Physiopathologie et thérapie des déficits sensoriels et moteurs, Université Montpellier 2 - Sciences et Techniques (UM2)-IFR76-Institut National de la Santé et de la Recherche Médicale (INSERM), Hamel, Christian, Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), The University of North Carolina at Chapel Hill-Carolina Center for the Genome Sciences, Université Montpellier 2 - Sciences et Techniques ( UM2 ) -IFR76-Institut National de la Santé et de la Recherche Médicale ( INSERM ), and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)

Subjects
Male, Cellular differentiation, GRB10 Adaptor Protein, MESH: Neurons, MESH : Promoter Regions, Genetic, MESH: Mice, Knockout, Histones, Mice, 0302 clinical medicine, MESH : Embryo, Mammalian, MESH : Female, MESH: Animals, Imprinting (psychology), Promoter Regions, Genetic, MESH: CpG Islands, Cells, Cultured, Genetics, Mice, Knockout, Neurons, MESH: Histones, 0303 health sciences, biology, MESH : Chromatin, General Neuroscience, Stem Cells, Polycomb Repressive Complex 2, Brain, MESH : GRB10 Adaptor Protein, Cell Differentiation, MESH : CpG Islands, Chromatin, Histone, MESH: Repressor Proteins, MESH : Stem Cells, Female, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], MESH : Repressor Proteins, MESH : Cell Differentiation, Bivalent chromatin, MESH: Cells, Cultured, MESH: Cell Differentiation, MESH : Male, MESH : Mice, Inbred C57BL, MESH: Stem Cells, General Biochemistry, Genetics and Molecular Biology, Bivalent (genetics), Article, MESH : Neurons, MESH: Chromatin, 03 medical and health sciences, Genomic Imprinting, MESH: Brain, MESH: Mice, Inbred C57BL, MESH : Mice, MESH : Cells, Cultured, MESH: Promoter Regions, Genetic, Animals, MESH : Histones, [SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], Molecular Biology, Gene, MESH: Mice, Alleles, 030304 developmental biology, General Immunology and Microbiology, MESH: Alleles, MESH: Embryo, Mammalian, MESH : Genomic Imprinting, Embryo, Mammalian, MESH: Male, MESH: Genomic Imprinting, Mice, Inbred C57BL, Repressor Proteins, MESH: GRB10 Adaptor Protein, MESH : Brain, [ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], biology.protein, MESH : Mice, Knockout, CpG Islands, MESH : Animals, Genomic imprinting, MESH : Alleles, MESH: Female, 030217 neurology & neurosurgery
Abstract

International audience; Genomic imprinting is a developmental mechanism that mediates parent-of-origin-specific expression in a subset of genes. How the tissue specificity of imprinted gene expression is controlled remains poorly understood. As a model to address this question, we studied Grb10, a gene that displays brain-specific expression from the paternal chromosome. Here, we show in the mouse that the paternal promoter region is marked by allelic bivalent chromatin enriched in both H3K4me2 and H3K27me3, from early embryonic stages onwards. This is maintained in all somatic tissues, but brain. The bivalent domain is resolved upon neural commitment, during the developmental window in which paternal expression is activated. Our data indicate that bivalent chromatin, in combination with neuronal factors, controls the paternal expression of Grb10 in brain. This finding highlights a novel mechanism to control tissue-specific imprinting.

Published
2008

5. The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5

Author

Matthieu Lacroix, Geneviève Rodier, Claude Sardet, Aphonse Le Cam, Eric Fabbrizio, Selma El Messaoudi, Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Institut de Génétique Moléculaire de Montpellier (IGMM), and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)

Subjects
MESH : Molecular Sequence Data, MESH: Protein Structure, Secondary, MESH: Amino Acid Sequence, MESH : Protein Methyltransferases, Biochemistry, Protein Structure, Secondary, MESH: Recombinant Proteins, Histones, 0302 clinical medicine, MESH: DNA Methylation, Genes, Reporter, MESH : Arginine, Histone methylation, Histone code, Luciferases, Glutathione Transferase, MESH: Histones, 0303 health sciences, MESH : Cell Nucleus, MESH : Chromatin, MESH : Amino Acid Sequence, MESH: Arginine, Nuclear Proteins, MESH : Protein Binding, MESH : Genes, Reporter, Chromatin, Recombinant Proteins, 3. Good health, 030220 oncology & carcinogenesis, Histone methyltransferase, MESH : Carrier Proteins, Protein Binding, MESH: Cell Nucleus, MESH : Glutathione Transferase, MESH: Cell Line, Tumor, MESH : Recombinant Proteins, Molecular Sequence Data, Scientific Report, MESH: Carrier Proteins, Biology, Arginine, MESH: Chromatin, Histone H4, 03 medical and health sciences, Histone H3, Histone H1, Histone arginine methylation, Cell Line, Tumor, Histone H2A, MESH: Protein Methyltransferases, Genetics, MESH: Protein Binding, Humans, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH : Histones, Amino Acid Sequence, Protein Methyltransferases, Molecular Biology, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, 030304 developmental biology, Cell Nucleus, MESH : Luciferases, MESH: Glutathione Transferase, MESH: Humans, MESH: Molecular Sequence Data, MESH : Cell Line, Tumor, MESH: Genes, Reporter, MESH : Humans, MESH : Nuclear Proteins, DNA Methylation, MESH: Luciferases, MESH : Protein Structure, Secondary, Carrier Proteins, MESH: Nuclear Proteins, MESH : DNA Methylation
Abstract

International audience; Protein arginine methyltransferase 5 (PRMT5) targets nuclear and cytoplasmic proteins. Here, we identified a nuclear protein, called cooperator of PRMT5 (COPR5), involved in the nuclear functions of PRMT5. COPR5 tightly binds to PRMT5, both in vitro and in living cells, but not to other members of the PRMT family. PRMT5 bound to COPR5 methylates histone H4 (R3) preferentially when compared with histone H3 (R8), suggesting that COPR5 modulates the substrate specificity of nuclear PRMT5-containing complexes, at least towards histones. Markedly, recombinant COPR5 binds to the amino terminus of histone H4 and is required to recruit PRMT5 to reconstituted nucleosomes in vitro. Consistently, COPR5 depletion in cells strongly reduces PRMT5 recruitment on chromatin at the PRMT5 target gene cyclin E1 (CCNE1) in vivo. Moreover, both COPR5 depletion and overexpression affect CCNE1 promoter expression. We propose that COPR5 is an important chromatin adaptor for PRMT5 to function on a subset of its target genes.

Published
2008

6. Glycogen synthase 2 is a novel target gene of peroxisome proliferator-activated receptors

Author

Mandard, Stéphane, Stienstra, Rinke, Escher, Pascal, Tan, Nguan Soon, Kim, Insook, Gonzalez, Frank, Wahli, Walter, Desvergne, Béatrice, Müller, Michael, Kersten, Sander, Nutrition, Metabolism and Genomics group and Nutrigenomics Consortium ( NMG ), Wageningen University and Research Centre [Wageningen] ( WUR ), Lipides - Nutrition - Cancer (U866) ( LNC ), Université de Bourgogne ( UB ) -Institut National de la Santé et de la Recherche Médicale ( INSERM ) -AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon ( ENSBANA ), Institute of Physiology, University of Basel ( Unibas ), Center for Integrative Genomics - Institute of Bioinformatics, Génopode ( CIG ), University of Lausanne, Laboratory of Metabolism, National Cancer Institute ( NIH ), This study was supported by the Netherlands Organization for Scientific Research (NWO), with additional support from the Dutch Diabetes Foundation, the Royal Netherlands Academy of Art and Sciences (KNAW), Wageningen Center for Food Sciences, the Center for Human Nutrigenomics, the Swiss National Science Foundation and the Human Frontier Science Program., Nutrition, Metabolism and Genomics group and Nutrigenomics Consortium (NMG), Wageningen University and Research [Wageningen] (WUR), Lipides - Nutrition - Cancer (U866) (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ecole Nationale Supérieure de Biologie Appliquée à la Nutrition et à l'Alimentation de Dijon (ENSBANA), University of Basel (Unibas), Center for Integrative Genomics - Institute of Bioinformatics, Génopode (CIG), Swiss Institute of Bioinformatics [Lausanne] (SIB), Université de Lausanne (UNIL)-Université de Lausanne (UNIL), National Cancer Institute [Bethesda] (NCI-NIH), and National Institutes of Health [Bethesda] (NIH)-National Institutes of Health [Bethesda] (NIH)

Subjects
MESH: DNA Primers, MESH: Rats, glycogen synthase 2, MESH: Peroxisome Proliferator-Activated Receptors, MESH : Hepatocytes, PPRE, liver, MESH: Mice, Knockout, PPAR, MESH: Chromatin, MESH : Gene Expression Regulation, Enzymologic, MESH: Hepatocytes, MESH: RNA, MESH : Mice, MESH : RNA, MESH: Animals, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Mice, HNF4α, MESH : Polymerase Chain Reaction, [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Glycogen Synthase, MESH : Chromatin, MESH : Rats, MESH: Transcription, Genetic, MESH: Gene Expression Regulation, Enzymologic, MESH : Transcription, Genetic, MESH: Polymerase Chain Reaction, MESH : Peroxisome Proliferator-Activated Receptors, adipose tissue, gene transcription, MESH : Mice, Knockout, MESH : DNA Primers, MESH : Animals, microarray, MESH : Glycogen Synthase
Abstract

International audience; Glycogen synthase 2 (Gys-2) is the ratelimiting enzyme in the storage of glycogen in liver and adipose tissue, yet little is known about regulation of Gys-2 transcription. The peroxisome proliferator-activated receptors (PPARs) are transcription factors involved in the regulation of lipid and glucose metabolism and might be hypothesized to govern glycogen synthesis as well. Here, we show that Gys-2 is a direct target gene of PPARalpha, PPARbeta/delta and PPARgamma. Expression of Gys-2 is significantly reduced in adipose tissue of PPARalpha-/-, PPARbeta/delta-/- and PPARgamma+/- mice. Furthermore, synthetic PPARbeta/delta, and gamma agonists markedly up-regulate Gys-2 mRNA and protein expression in mouse 3T3-L1 adipocytes. In liver, PPARalpha deletion leads to decreased glycogen levels in the refed state, which is paralleled by decreased expression of Gys-2 in fasted and refed state. Two putative PPAR response elements (PPREs) were identified in the mouse Gys-2 gene: one in the upstream promoter (DR-1prom) and one in intron 1 (DR-1int). It is shown that DR-1int is the response element for PPARs, while DR-1prom is the response element for Hepatic Nuclear Factor 4 alpha (HNF4alpha). In adipose tissue, which does not express HNF4alpha, DR-1prom is occupied by PPARbeta/delta and PPARgamma, yet binding does not translate into transcriptional activation of Gys-2. Overall, we conclude that mouse Gys-2 is a novel PPAR target gene and that transactivation by PPARs and HNF4alpha is mediated by two distinct response elements.

Published
2007

7. Differential histone modifications mark mouse imprinting control regions during spermatogenesis

Author

Katia Delaval, Saadi Khochbin, Jérôme Govin, Robert Feil, Sophie Rousseaux, Frédérique Cerqueira, Institut de Génétique Moléculaire de Montpellier (IGMM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Biologie moléculaire et cellulaire de la différenciation, Université Joseph Fourier - Grenoble 1 (UJF)-Institut Albert Bonniot-Institut National de la Santé et de la Recherche Médicale (INSERM), Salas, Danielle, Institut de Génétique Moléculaire de Montpellier ( IGMM ), Université de Montpellier ( UM ) -Centre National de la Recherche Scientifique ( CNRS ), Université Joseph Fourier - Grenoble 1 ( UJF ) -Institut Albert Bonniot-Institut National de la Santé et de la Recherche Médicale ( INSERM ), and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)

Subjects
Male, animal diseases, MESH : Blotting, Western, [ SDV.CAN ] Life Sciences [q-bio]/Cancer, Histones, Mice, 0302 clinical medicine, MESH: DNA Methylation, Histone methylation, MESH : Locus Control Region, MESH: Animals, Genetics, MESH: Chromatin Immunoprecipitation, MESH: Histones, 0303 health sciences, biology, MESH : Chromatin, General Neuroscience, virus diseases, Methylation, Chromatin, Histone, 030220 oncology & carcinogenesis, DNA methylation, MESH: Spermatogenesis, MESH: Computational Biology, Chromatin Immunoprecipitation, MESH: Locus Control Region, MESH : Sex Factors, MESH : Male, Blotting, Western, [SDV.CAN]Life Sciences [q-bio]/Cancer, General Biochemistry, Genetics and Molecular Biology, Article, MESH: Chromatin, 03 medical and health sciences, Genomic Imprinting, Sex Factors, MESH : Chromatin Immunoprecipitation, MESH : Spermatogenesis, MESH: Sex Factors, [SDV.CAN] Life Sciences [q-bio]/Cancer, MESH : Mice, Animals, MESH: Blotting, Western, MESH : Histones, Spermatogenesis, Molecular Biology, MESH: Mice, 030304 developmental biology, General Immunology and Microbiology, Computational Biology, MESH : Genomic Imprinting, DNA Methylation, Locus Control Region, MESH: Male, MESH: Genomic Imprinting, Acetylation, biology.protein, MESH : Animals, Genomic imprinting, Chromatin immunoprecipitation, MESH : DNA Methylation, MESH : Computational Biology
Abstract

International audience; Only some imprinting control regions (ICRs) acquire their DNA methylation in the male germ line. These imprints are protected against the global demethylation of the sperm genome following fertilisation, and are maintained throughout development. We find that in somatic cells and tissues, DNA methylation at these ICRs is associated with histone H4-lysine-20 and H3-lysine-9 trimethylation. The unmethylated allele, in contrast, has H3-lysine-4 dimethylation and H3 acetylation. These differential modifications are also detected at maternally methylated ICRs, and could be involved in the somatic maintenance of imprints. To explore whether the post-fertilisation protection of imprints relates to events during spermatogenesis, we assayed chromatin at stages preceding the global histone-to-protamine exchange. At these stages, H3-lysine-4 methylation and H3 acetylation are enriched at maternally methylated ICRs, but are absent at paternally methylated ICRs. H4 acetylation is enriched at all regions analysed. Thus, paternally and maternally methylated ICRs carry different histone modifications during the stages preceding the global histone-to-protamine exchange. These differences could influence the way ICRs are assembled into specific structures in late spermatogenesis, and may thus influence events after fertilisation.

Published
2007

8. RNAi-directed assembly of heterochromatin in fission yeast

Author

André Verdel, Danesh Moazed, Verdel, Andre, Department of cell biology, and Harvard Medical School [Boston] ( HMS )

Subjects
Euchromatin, MESH : Models, Genetic, [SDV.GEN] Life Sciences [q-bio]/Genetics, MESH : Models, Biological, MESH : RNA, Small Interfering, Biochemistry, Histone methylation, Histones, Structural Biology, Heterochromatin, MESH : RNA, RNA, Small Interfering, Heterochromatin assembly, Genetics, Genome, MESH : Chromatin, MESH : Histone Deacetylases, EZH2, Clr4, Chromatin, Transcriptional gene silencing, MESH : Lysine, MESH : RNA Replicase, RNA Interference, Epigenetics, RNA Polymerase II, MESH : RNA Polymerase II, RNA-induced transcriptional silencing, Biophysics, RITS, Biology, Methylation, Models, Biological, Histone Deacetylases, Schizosaccharomyces, Animals, MESH : Histones, Molecular Biology, RNA, Double-Stranded, Histone binding, Models, Genetic, MESH : Heterochromatin, Lysine, fungi, MESH : RNA, Double-Stranded, Cell Biology, MESH : Methylation, RNA-Dependent RNA Polymerase, MESH : Schizosaccharomyces, RNAi, RNA, Heterochromatin protein 1, MESH : Animals, MESH : RNA Interference, MESH : Genome, [ SDV.GEN ] Life Sciences [q-bio]/Genetics
Abstract

International audience; Heterochromatin is an epigenetically heritable and conserved feature of eukaryotic chromosomes with important roles in chromosome segregation, genome stability, and gene regulation. The formation of heterochromatin involves an ordered array of chromatin changes, including histone deacetylation, histone H3-lysine 9 methylation, and recruitment of histone binding proteins such as Swi6/HP1. Recent discoveries have uncovered a role for the RNA interference (RNAi) pathway in heterochromatin assembly in the fission yeast Schizosaccharomyces pombe and other eukaryotes. Purification of two RNAi complexes, RITS and RDRC, from fission yeast has provided further insight into the mechanism of RNAi-mediated heterochromatin assembly. These discoveries have given rise to a model in which small interfering RNA molecules act as specificity factors that initiate epigenetic chromatin modifications and double strand RNA synthesis at specific chromosome regions.

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