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  1 / 103 MEDLINE  
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[PMID]:26759081
[Au] Autor:Wani AH; Boettiger AN; Schorderet P; Ergun A; Münger C; Sadreyev RI; Zhuang X; Kingston RE; Francis NJ
[Ad] Endereço:Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts, USA.
[Ti] Título:Chromatin topology is coupled to Polycomb group protein subnuclear organization.
[So] Source:Nat Commun;7:10291, 2016 Jan 13.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The genomes of metazoa are organized at multiple scales. Many proteins that regulate genome architecture, including Polycomb group (PcG) proteins, form subnuclear structures. Deciphering mechanistic links between protein organization and chromatin architecture requires precise description and mechanistic perturbations of both. Using super-resolution microscopy, here we show that PcG proteins are organized into hundreds of nanoscale protein clusters. We manipulated PcG clusters by disrupting the polymerization activity of the sterile alpha motif (SAM) of the PcG protein Polyhomeotic (Ph) or by increasing Ph levels. Ph with mutant SAM disrupts clustering of endogenous PcG complexes and chromatin interactions while elevating Ph level increases cluster number and chromatin interactions. These effects can be captured by molecular simulations based on a previously described chromatin polymer model. Both perturbations also alter gene expression. Organization of PcG proteins into small, abundant clusters on chromatin through Ph SAM polymerization activity may shape genome architecture through chromatin interactions.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Proteínas de Ligação a DNA/metabolismo
Proteínas de Drosophila/metabolismo
Espaço Intranuclear/metabolismo
Complexo Repressor Polycomb 1/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Linhagem Celular
Imunoprecipitação da Cromatina
Drosophila
Imunofluorescência
Microscopia
Simulação de Dinâmica Molecular
Imagem Óptica
Proteínas do Grupo Polycomb/metabolismo
Polímeros
Estrutura Quaternária de Proteína
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Análise de Sequência de DNA
Análise de Sequência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (DNA-Binding Proteins); 0 (Drosophila Proteins); 0 (Polycomb-Group Proteins); 0 (Polymers); 146888-72-4 (polyhomeotic protein, Drosophila); EC 2.3.2.27 (Polycomb Repressive Complex 1)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170324
[Lr] Data última revisão:
170324
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160114
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms10291


  2 / 103 MEDLINE  
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[PMID]:26703574
[Au] Autor:Wang S; Liu S
[Ad] Endereço:School of Information Science and Engineering, Yunnan University, Kunming 650504, China. sfwang_66@ynu.edu.cn.
[Ti] Título:Protein Sub-Nuclear Localization Based on Effective Fusion Representations and Dimension Reduction Algorithm LDA.
[So] Source:Int J Mol Sci;16(12):30343-61, 2015 Dec 19.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:An effective representation of a protein sequence plays a crucial role in protein sub-nuclear localization. The existing representations, such as dipeptide composition (DipC), pseudo-amino acid composition (PseAAC) and position specific scoring matrix (PSSM), are insufficient to represent protein sequence due to their single perspectives. Thus, this paper proposes two fusion feature representations of DipPSSM and PseAAPSSM to integrate PSSM with DipC and PseAAC, respectively. When constructing each fusion representation, we introduce the balance factors to value the importance of its components. The optimal values of the balance factors are sought by genetic algorithm. Due to the high dimensionality of the proposed representations, linear discriminant analysis (LDA) is used to find its important low dimensional structure, which is essential for classification and location prediction. The numerical experiments on two public datasets with KNN classifier and cross-validation tests showed that in terms of the common indexes of sensitivity, specificity, accuracy and MCC, the proposed fusing representations outperform the traditional representations in protein sub-nuclear localization, and the representation treated by LDA outperforms the untreated one.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular
Algoritmos
Espaço Intranuclear/metabolismo
[Mh] Termos MeSH secundário: Dipeptídeos/metabolismo
Modelos Teóricos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Dipeptides)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151226
[St] Status:MEDLINE
[do] DOI:10.3390/ijms161226237


  3 / 103 MEDLINE  
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[PMID]:25891951
[Au] Autor:Tatemichi Y; Shibazaki M; Yasuhira S; Kasai S; Tada H; Oikawa H; Suzuki Y; Takikawa Y; Masuda T; Maesawa C
[Ad] Endereço:Department of Tumor Biology, Institute of Biomedical Sciences, Iwate Medical University, Yahaba-cho, Japan.
[Ti] Título:Nucleus accumbens associated 1 is recruited within the promyelocytic leukemia nuclear body through SUMO modification.
[So] Source:Cancer Sci;106(7):848-56, 2015 Jul.
[Is] ISSN:1349-7006
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nucleus accumbens associated 1 (NACC1) is a cancer-associated BTB/POZ (pox virus and zinc finger/bric-a-brac tramtrack broad complex) gene, and is involved in several cellular functions in neurons, cancer and stem cells. Some of the BTB/POZ proteins associated with cancer biology are SUMOylated, which appears to play an important role in transcription regulation. We show that NACC1 is SUMOylated on a phylogenetically conserved lysine (K167) out of three consensus SUMOylation motif sites. Amino acid substitution in the SIM sequence (SIM/M) within the BTB/POZ domain partially reduced K167 SUMOylation activity of NACC1. Overexpression of GFP-NACC1 fusion protein leads to formation of discrete nuclear foci similar to promyelocytic leukemia nuclear bodies (PML-NB), which colocalized with SUMO paralogues (SUMO1/2/3). Both NACC1 nuclear body formation and colocalization with SUMO paralogues were completely suppressed in the GFP-NACC1-SIM/M mutant, whereas they were partially maintained in the NACC1 K167R mutant. Confocal immunofluorescence analysis showed that endogenous and exogenous NACC1 proteins colocalized with endogenous PML protein. A pull-down assay revealed that the consensus motifs of the SUMO acceptor site at K167 and the SIM within the BTB/POZ domain were both necessary for efficient binding to PML protein. Our study demonstrates that NACC1 can be modified by SUMO paralogues, and cooperates with PML protein.
[Mh] Termos MeSH primário: Proteínas de Neoplasias/metabolismo
Proteínas Nucleares/metabolismo
Proteínas Repressoras/metabolismo
Sumoilação
Fatores de Transcrição/metabolismo
Proteínas Supressoras de Tumor/metabolismo
Enzimas de Conjugação de Ubiquitina/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Células HeLa
Seres Humanos
Espaço Intranuclear/metabolismo
Leucemia Promielocítica Aguda/metabolismo
Leucemia Promielocítica Aguda/patologia
Células MCF-7
Dados de Sequência Molecular
Proteína da Leucemia Promielocítica
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NACC1 protein, human); 0 (Neoplasm Proteins); 0 (Nuclear Proteins); 0 (Promyelocytic Leukemia Protein); 0 (Repressor Proteins); 0 (Transcription Factors); 0 (Tumor Suppressor Proteins); 143220-95-5 (PML protein, human); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 6.3.2.- (ubiquitin-conjugating enzyme UBC9)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150421
[St] Status:MEDLINE
[do] DOI:10.1111/cas.12680


  4 / 103 MEDLINE  
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[PMID]:25557830
[Au] Autor:Lee S; Lee TA; Lee E; Kang S; Park A; Kim SW; Park HJ; Yoon JH; Ha SJ; Park T; Lee JS; Cheon JH; Park B
[Ad] Endereço:Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, 50 Yonsei-ro, Seodaemun-gu, Seoul 120-749, South Korea.
[Ti] Título:Identification of a subnuclear body involved in sequence-specific cytokine RNA processing.
[So] Source:Nat Commun;6:5791, 2015 Jan 05.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Processing of interleukin RNAs must be tightly controlled during the immune response. Here we report that a subnuclear body called the interleukin-6 and -10 splicing activating compartment (InSAC) is a nuclear site of cytokine RNA production and stability. Tat-activating regulatory DNA-binding protein-43 (TDP-43) acts as an InSAC scaffold that selectively associates with IL-6 and IL-10 RNAs in a sequence-specific manner. TDP-43 also recruits key spliceosomal components from Cajal bodies. LPS induces posttranslational modifications of TDP-43; in particular, TDP-43 ubiquitination provides a driving force for InSAC formation. As a consequence, in vivo depletion of TDP-43 leads to a dramatic reduction in the RNA processing and the protein levels of IL-6 in serum. Collectively, our findings highlight the importance of TDP-43-mediated InSAC biogenesis in immune regulation.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/metabolismo
Imunidade Celular/genética
Espaço Intranuclear/fisiologia
Processamento Pós-Transcricional do RNA/fisiologia
Spliceossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Ensaio de Desvio de Mobilidade Eletroforética
Ensaio de Imunoadsorção Enzimática
Seres Humanos
Immunoblotting
Imunoprecipitação
Hibridização in Situ Fluorescente
Interleucina-10/metabolismo
Interleucina-6/metabolismo
Lipopolissacarídeos
Camundongos
Camundongos Endogâmicos C57BL
Interferência de RNA
Reação em Cadeia da Polimerase em Tempo Real
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Interleukin-6); 0 (Lipopolysaccharides); 0 (TDP-43 protein, mouse); 130068-27-8 (Interleukin-10)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:170930
[Lr] Data última revisão:
170930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150106
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms6791


  5 / 103 MEDLINE  
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[PMID]:25739295
[Au] Autor:Khodiuchenko TA; Krasikova AV
[Ti] Título:[Cajal bodies and histone locus bodies: molecular structure and function].
[So] Source:Ontogenez;45(6):363-79, 2014 Nov-Dec.
[Is] ISSN:0475-1450
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The review provides modern classification of evolutionarily conserved coilin-containing nuclear bodies of somatic and germ cells that is based on the characteristic features of their molecular composition and the nature of their functions. The main differences between Cajal bodies and histone locus bodies, which are involved in the biogenesis of small nuclear spliceosomal and nucleolar RNAs and in the 3'-end processing of histone precursor messenger RNA, respectively, are considered. It is shown that a significant contribution to the investigation of the diversity of coilin-containing bodies was made by the studies on the architecture of the RNA processing machinery in oocyte nuclei in a number of model organisms. The characteristics features of the molecular composition of coilin-containing bodies in the nuclei of growing oocytes (the so-called germinal vesicles) of vertebrates, including amphibians and birds, are described.
[Mh] Termos MeSH primário: Loci Gênicos/fisiologia
Histonas/metabolismo
Espaço Intranuclear/metabolismo
Oócitos/metabolismo
Precursores de RNA/metabolismo
Processamento Pós-Transcricional do RNA/fisiologia
[Mh] Termos MeSH secundário: Anfíbios/genética
Anfíbios/metabolismo
Animais
Aves/genética
Aves/metabolismo
Feminino
Histonas/genética
Masculino
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Precursores de RNA/genética
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Histones); 0 (Nuclear Proteins); 0 (RNA Precursors); 136882-81-0 (p80-coilin)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:150305
[Lr] Data última revisão:
150305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150306
[St] Status:MEDLINE


  6 / 103 MEDLINE  
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[PMID]:25342201
[Au] Autor:Grand RS; Pichugina T; Gehlen LR; Jones MB; Tsai P; Allison JR; Martienssen R; O'Sullivan JM
[Ad] Endereço:Liggins institute, University of Auckland, Grafton Auckland 1032, NZ Institute of Natural and Mathematical Sciences, Massey University, Albany, Auckland 0745, NZ.
[Ti] Título:Chromosome conformation maps in fission yeast reveal cell cycle dependent sub nuclear structure.
[So] Source:Nucleic Acids Res;42(20):12585-99, 2014 Nov 10.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Successful progression through the cell cycle requires spatial and temporal regulation of gene transcript levels and the number, positions and condensation levels of chromosomes. Here we present a high resolution survey of genome interactions in Schizosaccharomyces pombe using synchronized cells to investigate cell cycle dependent changes in genome organization and transcription. Cell cycle dependent interactions were captured between and within S. pombe chromosomes. Known features of genome organization (e.g. the clustering of telomeres and retrotransposon long terminal repeats (LTRs)) were observed throughout the cell cycle. There were clear correlations between transcript levels and chromosomal interactions between genes, consistent with a role for interactions in transcriptional regulation at specific stages of the cell cycle. In silico reconstructions of the chromosome organization within the S. pombe nuclei were made by polymer modeling. These models suggest that groups of genes with high and low, or differentially regulated transcript levels have preferred positions within the S. pombe nucleus. We conclude that the S. pombe nucleus is spatially divided into functional sub-nuclear domains that correlate with gene activity. The observation that chromosomal interactions are maintained even when chromosomes are fully condensed in M phase implicates genome organization in epigenetic inheritance and bookmarking.
[Mh] Termos MeSH primário: Ciclo Celular/genética
Núcleo Celular/genética
Cromossomos Fúngicos
Regulação Fúngica da Expressão Gênica
Schizosaccharomyces/genética
[Mh] Termos MeSH secundário: Genoma Fúngico
Espaço Intranuclear
Sequências Repetidas Terminais
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1503
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141025
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gku965


  7 / 103 MEDLINE  
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[PMID]:25056310
[Au] Autor:Thévenin A; Ein-Dor L; Ozery-Flato M; Shamir R
[Ad] Endereço:Genome Informatics, Faculty of Technology and Institute for Bioinformatics, Center for Biotechnology (CeBiTec), Bielefeld University, Bielefeld 33615, Germany IBM Research-Haifa, Mount Carmel, Haifa 3498825, Israel.
[Ti] Título:Functional gene groups are concentrated within chromosomes, among chromosomes and in the nuclear space of the human genome.
[So] Source:Nucleic Acids Res;42(15):9854-61, 2014 Sep.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Genomes undergo changes in organization as a result of gene duplications, chromosomal rearrangements and local mutations, among other mechanisms. In contrast to prokaryotes, in which genes of a common function are often organized in operons and reside contiguously along the genome, most eukaryotes show much weaker clustering of genes by function, except for few concrete functional groups. We set out to check systematically if there is a relation between gene function and gene organization in the human genome. We test this question for three types of functional groups: pairs of interacting proteins, complexes and pathways. We find a significant concentration of functional groups both in terms of their distance within the same chromosome and in terms of their dispersal over several chromosomes. Moreover, using Hi-C contact map of the tendency of chromosomal segments to appear close in the 3D space of the nucleus, we show that members of the same functional group that reside on distinct chromosomes tend to co-localize in space. The result holds for all three types of functional groups that we tested. Hence, the human genome shows substantial concentration of functional groups within chromosomes and across chromosomes in space.
[Mh] Termos MeSH primário: Núcleo Celular/genética
Cromossomos Humanos
Genes
Genoma Humano
[Mh] Termos MeSH secundário: Seres Humanos
Espaço Intranuclear
Mapeamento de Interação de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1412
[Cu] Atualização por classe:150805
[Lr] Data última revisão:
150805
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140725
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gku667


  8 / 103 MEDLINE  
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[PMID]:24516149
[Au] Autor:Shin J; Wang S; Deng W; Wu J; Gao J; Zhong XP
[Ad] Endereço:Departments of Pediatrics and Immunology, Duke University Medical Center, Durham, NC 27710.
[Ti] Título:Mechanistic target of rapamycin complex 1 is critical for invariant natural killer T-cell development and effector function.
[So] Source:Proc Natl Acad Sci U S A;111(8):E776-83, 2014 Feb 25.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mechanisms that control invariant natural killer T (iNKT)-cell development and function are still poorly understood. The mechanistic or mammalian target of rapamycin (mTOR) integrates various environmental signals/cues to regulate cell growth, proliferation, metabolism, and survival. We report here that ablation of mTOR complex 1 (mTORC1) signaling by conditionally deleting Raptor causes severe defects in iNKT-cell development at early stages, leading to drastic reductions in iNKT-cell numbers in the thymus and periphery. In addition, loss of Raptor impairs iNKT-cell proliferation and production of cytokines upon α-galactosylceramide stimulation in vitro and in vivo, and inhibits liver inflammation in an iNKT cell-mediated hepatitis model. Furthermore, Raptor deficiency and rapamycin treatment lead to aberrant intracellular localization and functional impairment of promyelocytic leukemia zinc-finger, a transcription factor critical for iNKT-cell development and effector programs. Our findings define an essential role of mTORC1 to direct iNKT-cell lineage development and effector function.
[Mh] Termos MeSH primário: Diferenciação Celular/imunologia
Fatores de Transcrição Kruppel-Like/imunologia
Complexos Multiproteicos/imunologia
Células T Matadoras Naturais/imunologia
Serina-Treonina Quinases TOR/imunologia
Timócitos/imunologia
[Mh] Termos MeSH secundário: Análise de Variância
Animais
Western Blotting
Transplante de Medula Óssea
Bromodesoxiuridina
Morte Celular/imunologia
Proliferação Celular
Imunoprecipitação da Cromatina
Primers do DNA/genética
Citometria de Fluxo
Genes Codificadores dos Receptores de Linfócitos T/genética
Espaço Intranuclear/metabolismo
Alvo Mecanístico do Complexo 1 de Rapamicina
Camundongos
Camundongos Knockout
Microscopia de Fluorescência
Proteína com Dedos de Zinco da Leucemia Promielocítica
Reação em Cadeia da Polimerase em Tempo Real
Estatísticas não Paramétricas
Timócitos/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA Primers); 0 (Kruppel-Like Transcription Factors); 0 (Multiprotein Complexes); 0 (Promyelocytic Leukemia Zinc Finger Protein); 0 (Zbtb16 protein, mouse); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1); G34N38R2N1 (Bromodeoxyuridine)
[Em] Mês de entrada:1404
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140212
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1315435111


  9 / 103 MEDLINE  
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[PMID]:24380594
[Au] Autor:Aumiller WM; Davis BW; Keating CD
[Ad] Endereço:Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania, USA.
[Ti] Título:Phase separation as a possible means of nuclear compartmentalization.
[So] Source:Int Rev Cell Mol Biol;307:109-49, 2014.
[Is] ISSN:1937-6448
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The nucleus is perhaps the most familiar organelle within eukaryotic cells, serving as a compartment to house the genetic material. The nuclear volume is subdivided into a variety of functional and dynamic nuclear bodies not separated from the nucleoplasm by membranes. It has been hypothesized that aqueous phase separation brought about by macromolecular crowding may be in part responsible for these intranuclear compartments. This chapter discusses macromolecular solution chemistry with regard to several common types of phase separation in polymer solutions as well as to recent evidence that suggests that cytoplasmic and nuclear bodies may exist as liquid phases. We then examine the functional significance of phase separation and how it may serve as a means of compartmentalizing various nuclear activities, and describe recent studies that have used simple model systems to generate coexisting aqueous phase compartments, concentrate molecules within them, and perform localized biochemical reactions.
[Mh] Termos MeSH primário: Espaço Intranuclear/fisiologia
Modelos Biológicos
[Mh] Termos MeSH secundário: Animais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; REVIEW
[Em] Mês de entrada:1408
[Cu] Atualização por classe:160518
[Lr] Data última revisão:
160518
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140102
[St] Status:MEDLINE


  10 / 103 MEDLINE  
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[PMID]:24191010
[Au] Autor:Jakociunas T; Domange Jordö M; Aït Mebarek M; Bünner CM; Verhein-Hansen J; Oddershede LB; Thon G
[Ad] Endereço:Department of Biology, University of Copenhagen, DK-2200 Copenhagen, Denmark.
[Ti] Título:Subnuclear relocalization and silencing of a chromosomal region by an ectopic ribosomal DNA repeat.
[So] Source:Proc Natl Acad Sci U S A;110(47):E4465-73, 2013 Nov 19.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Our research addresses the relationship between subnuclear localization and gene expression in fission yeast. We observed the relocalization of a heterochromatic region, the mating-type region, from its natural location at the spindle-pole body to the immediate vicinity of the nucleolus. Relocalization occurred in response to a DNA rearrangement replacing a boundary element (IR-R) with a ribosomal DNA repeat (rDNA-R). Gene expression was strongly silenced in the relocalized mating-type region through mechanisms that differ from those operating in wild type. Also different from the wild-type situation, programmed recombination events failed to take place in the rDNA-R mutant. Increased silencing and perinucleolar localization depended on Reb1, a DNA-binding protein with cognate sites in the rDNA. Reb1 was recently shown to mediate long-range interchromosomal interactions in the nucleus through dimerization, providing a mechanism for the observed relocalization. Replacing the full rDNA repeat with Reb1-binding sites, and using mutants lacking the histone H3K9 methyltransferase Clr4, indicated that the relocalized region was silenced redundantly by heterochromatin and another mechanism, plausibly antisense transcription, achieving a high degree of repression in the rDNA-R strain.
[Mh] Termos MeSH primário: DNA Ribossômico/genética
Proteínas de Ligação a DNA/metabolismo
Inativação Gênica
Heterocromatina/fisiologia
Espaço Intranuclear/metabolismo
Proteínas de Schizosaccharomyces pombe/metabolismo
Schizosaccharomyces/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação/genética
Proteínas de Ligação a DNA/genética
Reação em Cadeia da Polimerase Multiplex
Sequências Repetitivas de Ácido Nucleico/genética
Schizosaccharomyces/genética
Proteínas de Schizosaccharomyces pombe/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Ribosomal); 0 (DNA-Binding Proteins); 0 (Heterochromatin); 0 (Schizosaccharomyces pombe Proteins); 0 (Transcription Factors); 0 (reb1 protein, S pombe)
[Em] Mês de entrada:1401
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131106
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1315581110



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