Base de dados : MEDLINE
Pesquisa : A11.284.430.106.279.345.190.160.180 [Categoria DeCS]
Referências encontradas : 33771 [refinar]
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[PMID]:29208012
[Au] Autor:Pereira A; Paro R
[Ad] Endereço:Department of Biosystems Science and Engineering, ETH Zurich, 4058, Basel, Switzerland.
[Ti] Título:Pho dynamically interacts with Spt5 to facilitate transcriptional switches at the hsp70 locus.
[So] Source:Epigenetics Chromatin;10(1):57, 2017 12 06.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Numerous target genes of the Polycomb group (PcG) are transiently activated by a stimulus and subsequently repressed. However, mechanisms by which PcG proteins regulate such target genes remain elusive. RESULTS: We employed the heat shock-responsive hsp70 locus in Drosophila to study the chromatin dynamics of PRC1 and its interplay with known regulators of the locus before, during and after heat shock. We detected mutually exclusive binding patterns for HSF and PRC1 at the hsp70 locus. We found that Pleiohomeotic (Pho), a DNA-binding PcG member, dynamically interacts with Spt5, an elongation factor. The dynamic interaction switch between Pho and Spt5 is triggered by the recruitment of HSF to chromatin. Mutation in the protein-protein interaction domain (REPO domain) of Pho interferes with the dynamics of its interaction with Spt5. The transcriptional kinetics of the heat shock response is negatively affected by a mutation in the REPO domain of Pho. CONCLUSIONS: We propose that a dynamic interaction switch between PcG proteins and an elongation factor enables stress-inducible genes to efficiently switch between ON/OFF states in the presence/absence of the activating stimulus.
[Mh] Termos MeSH primário: Proteínas Cromossômicas não Histona/metabolismo
Proteínas de Drosophila/metabolismo
Proteínas de Choque Térmico HSP70/genética
Proteínas do Grupo Polycomb/metabolismo
Fatores de Elongação da Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular
Cromatina/metabolismo
Proteínas de Drosophila/química
Drosophila melanogaster
Resposta ao Choque Térmico
Proteínas do Grupo Polycomb/química
Ligação Proteica
Homologia de Sequência de Aminoácidos
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (Drosophila Proteins); 0 (HSP70 Heat-Shock Proteins); 0 (Polycomb-Group Proteins); 0 (Transcriptional Elongation Factors); 0 (pho protein, Drosophila); 138673-72-0 (SPT5 transcriptional elongation factor)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE
[do] DOI:10.1186/s13072-017-0166-9


  2 / 33771 MEDLINE  
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[PMID]:28747224
[Au] Autor:Schröder C; Leitão E; Wallner S; Schmitz G; Klein-Hitpass L; Sinha A; Jöckel KH; Heilmann-Heimbach S; Hoffmann P; Nöthen MM; Steffens M; Ebert P; Rahmann S; Horsthemke B
[Ad] Endereço:Genome Informatics, Institute of Human Genetics, University of Duisburg-Essen, University Hospital Essen, Essen, Germany.
[Ti] Título:Regions of common inter-individual DNA methylation differences in human monocytes: genetic basis and potential function.
[So] Source:Epigenetics Chromatin;10(1):37, 2017 07 26.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: There is increasing evidence for inter-individual methylation differences at CpG dinucleotides in the human genome, but the regional extent and function of these differences have not yet been studied in detail. For identifying regions of common methylation differences, we used whole genome bisulfite sequencing data of monocytes from five donors and a novel bioinformatic strategy. RESULTS: We identified 157 differentially methylated regions (DMRs) with four or more CpGs, almost none of which has been described before. The DMRs fall into different chromatin states, where methylation is inversely correlated with active, but not repressive histone marks. However, methylation is not correlated with the expression of associated genes. High-resolution single nucleotide polymorphism (SNP) genotyping of the five donors revealed evidence for a role of cis-acting genetic variation in establishing methylation patterns. To validate this finding in a larger cohort, we performed genome-wide association studies (GWAS) using SNP genotypes and 450k array methylation data from blood samples of 1128 individuals. Only 30/157 (19%) DMRs include at least one 450k CpG, which shows that these arrays miss a large proportion of DNA methylation variation. In most cases, the GWAS peak overlapped the CpG position, and these regions are enriched for CREB group, NF-1, Sp100 and CTCF binding motifs. In two cases, there was tentative evidence for a trans-effect by KRAB zinc finger proteins. CONCLUSIONS: Allele-specific DNA methylation occurs in discrete chromosomal regions and is driven by genetic variation in cis and trans, but in general has little effect on gene expression.
[Mh] Termos MeSH primário: Metilação de DNA
Motivos de Nucleotídeos
Polimorfismo de Nucleotídeo Único
[Mh] Termos MeSH secundário: Células Cultivadas
Cromatina/genética
Ilhas de CpG
Seres Humanos
Monócitos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1186/s13072-017-0144-2


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[PMID]:27777629
[Au] Autor:Lau AC; Zhu KP; Brouhard EA; Davis MB; Csankovszki G
[Ad] Endereço:Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N. University Ave., Ann Arbor, MI 48109-1048 USA ; Genome Technologies, The Jackson Laboratory for Genomic Medicine, Farmington, CT 06032 USA.
[Ti] Título:An H4K16 histone acetyltransferase mediates decondensation of the X chromosome in males.
[So] Source:Epigenetics Chromatin;9:44, 2016.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In , in order to equalize gene expression between the sexes and balance X and autosomal expression, two steps are believed to be required. First, an unknown mechanism is hypothesized to upregulate the X chromosome in both sexes. This mechanism balances the X to autosomal expression in males, but creates X overexpression in hermaphrodites. Therefore, to restore the balance, hermaphrodites downregulate gene expression twofold on both X chromosomes. While many studies have focused on X chromosome downregulation, the mechanism of X upregulation is not known. RESULTS: To gain more insight into X upregulation, we studied the effects of chromatin condensation and histone acetylation on gene expression levels in male . We have found that the H4K16 histone acetyltransferase MYS-1/Tip60 mediates dramatic decondensation of the male X chromosome as measured by FISH. However, RNA-seq analysis revealed that MYS-1 contributes only slightly to upregulation of gene expression on the X chromosome. These results suggest that the level of chromosome decondensation does not necessarily correlate with the degree of gene expression change in vivo. Furthermore, the X chromosome is more sensitive to MYS-1-mediated decondensation than the autosomes, despite similar levels of H4K16ac on all chromosomes, as measured by ChIP-seq. H4K16ac levels weakly correlate with gene expression levels on both the X and the autosomes, but highly expressed genes on the X chromosome do not contain exceptionally high levels of H4K16ac. CONCLUSION: These results indicate that H4K16ac and chromosome decondensation influence regulation of the male X chromosome; however, they do not fully account for the high levels of gene expression observed on the X chromosomes.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Histona Acetiltransferases/metabolismo
Cromossomo X/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Cromatina/metabolismo
Montagem e Desmontagem da Cromatina
Imunoprecipitação da Cromatina
Compensação de Dosagem (Genética)
Expressão Gênica
Histona Acetiltransferases/genética
Histonas/metabolismo
Hibridização in Situ Fluorescente
Masculino
Análise de Sequência de DNA
Cromossomo X/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Chromatin); 0 (Histones); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (MYS-1 protein, C elegans)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


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[PMID]:27777628
[Au] Autor:Brueckner L; van Arensbergen J; Akhtar W; Pagie L; van Steensel B
[Ad] Endereço:Division of Gene Regulation, Netherlands Cancer Institute, Amsterdam, The Netherlands.
[Ti] Título:High-throughput assessment of context-dependent effects of chromatin proteins.
[So] Source:Epigenetics Chromatin;9:43, 2016.
[Is] ISSN:1756-8935
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Chromatin proteins control gene activity in a concerted manner. We developed a high-throughput assay to study the effects of the local chromatin environment on the regulatory activity of a protein of interest. The assay combines a previously reported multiplexing strategy based on barcoded randomly integrated reporters with Gal4-mediated tethering. We applied the assay to heterochromatin protein 1a (HP1a), which is mostly known as a repressive protein but has also been linked to transcriptional activation. RESULTS: Recruitment to over 1000 genomic locations revealed that HP1a is a potent repressor able to silence even highly expressing reporter genes. However, the local chromatin context can modulate HP1a function. In pericentromeric regions, HP1a-induced repression was enhanced by twofold. In regions marked by a H3K36me3-rich chromatin signature, HP1a-dependent silencing was significantly decreased. We found no evidence for an activating function of HP1a in our experimental system. Furthermore, we did not observe stable transmission of repression over mitotic divisions after loss of targeted HP1a. CONCLUSIONS: The multiplexed tethered reporter assay should be applicable to a large number of chromatin proteins and will be a useful tool to dissect combinatorial regulatory interactions in chromatin.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Proteínas Cromossômicas não Histona/genética
Proteínas de Drosophila/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Proteínas Cromossômicas não Histona/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/genética
Drosophila melanogaster/metabolismo
Inativação Gênica
Histonas/metabolismo
Plasmídeos/genética
Plasmídeos/metabolismo
Elongação da Transcrição Genética
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Transfecção
[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 (Chromosomal Proteins, Non-Histone); 0 (Drosophila Proteins); 0 (GAL4 protein, Drosophila); 0 (Histones); 0 (Transcription Factors)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180310
[Lr] Data última revisão:
180310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  5 / 33771 MEDLINE  
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[PMID]:29339721
[Au] Autor:Kilic S; Felekyan S; Doroshenko O; Boichenko I; Dimura M; Vardanyan H; Bryan LC; Arya G; Seidel CAM; Fierz B
[Ad] Endereço:Laboratory of Biophysical Chemistry of Macromolecules, Institute of Chemical Sciences and Engineering (ISIC), Ecole Polytechnique Fédérale de Lausanne (EPFL), 1015, Lausanne, Switzerland.
[Ti] Título:Single-molecule FRET reveals multiscale chromatin dynamics modulated by HP1α.
[So] Source:Nat Commun;9(1):235, 2018 01 16.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The dynamic architecture of chromatin fibers, a key determinant of genome regulation, is poorly understood. Here, we employ multimodal single-molecule Förster resonance energy transfer studies to reveal structural states and their interconversion kinetics in chromatin fibers. We show that nucleosomes engage in short-lived (micro- to milliseconds) stacking interactions with one of their neighbors. This results in discrete tetranucleosome units with distinct interaction registers that interconvert within hundreds of milliseconds. Additionally, we find that dynamic chromatin architecture is modulated by the multivalent architectural protein heterochromatin protein 1α (HP1α), which engages methylated histone tails and thereby transiently stabilizes stacked nucleosomes. This compacted state nevertheless remains dynamic, exhibiting fluctuations on the timescale of HP1α residence times. Overall, this study reveals that exposure of internal DNA sites and nucleosome surfaces in chromatin fibers is governed by an intrinsic dynamic hierarchy from micro- to milliseconds, allowing the gene regulation machinery to access compact chromatin.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Transferência Ressonante de Energia de Fluorescência/métodos
Nucleossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Cromatina/química
Cromatina/genética
DNA/química
DNA/genética
DNA/metabolismo
Regulação da Expressão Gênica
Histonas/metabolismo
Cinética
Metilação
Microscopia de Fluorescência
Conformação Molecular
Conformação de Ácido Nucleico
Nucleossomos/química
Nucleossomos/genética
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (Histones); 0 (Nucleosomes); 107283-02-3 (heterochromatin-specific nonhistone chromosomal protein HP-1); 9007-49-2 (DNA)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02619-5


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[PMID]:28467304
[Au] Autor:Hansen AS; Pustova I; Cattoglio C; Tjian R; Darzacq X
[Ad] Endereço:Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
[Ti] Título:CTCF and cohesin regulate chromatin loop stability with distinct dynamics.
[So] Source:Elife;6, 2017 05 03.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Folding of mammalian genomes into spatial domains is critical for gene regulation. The insulator protein CTCF and cohesin control domain location by folding domains into loop structures, which are widely thought to be stable. Combining genomic and biochemical approaches we show that CTCF and cohesin co-occupy the same sites and physically interact as a biochemically stable complex. However, using single-molecule imaging we find that CTCF binds chromatin much more dynamically than cohesin (~1-2 min vs. ~22 min residence time). Moreover, after unbinding, CTCF quickly rebinds another cognate site unlike cohesin for which the search process is long (~1 min vs. ~33 min). Thus, CTCF and cohesin form a rapidly exchanging 'dynamic complex' rather than a typical stable complex. Since CTCF and cohesin are required for loop domain formation, our results suggest that chromatin loops are dynamic and frequently break and reform throughout the cell cycle.
[Mh] Termos MeSH primário: Fator de Ligação a CCCTC/metabolismo
Proteínas de Ciclo Celular/metabolismo
Cromatina/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Cinética
Camundongos
Ligação Proteica
Mapeamento de Interação de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (CCCTC-Binding Factor); 0 (Cell Cycle Proteins); 0 (Chromatin); 0 (Chromosomal Proteins, Non-Histone); 0 (cohesins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  7 / 33771 MEDLINE  
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[PMID]:28747316
[Au] Autor:Suresh S; Markossian S; Osmani AH; Osmani SA
[Ad] Endereço:Department of Molecular Genetics, The Ohio State University, Columbus, OH.
[Ti] Título:Mitotic nuclear pore complex segregation involves Nup2 in .
[So] Source:J Cell Biol;216(9):2813-2826, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transport through nuclear pore complexes (NPCs) during interphase is facilitated by the nucleoporin Nup2 via its importin α- and Ran-binding domains. However, and vertebrate Nup2 also locate to chromatin during mitosis, suggestive of mitotic functions. In this study, we report that Nup2 is required for mitotic NPC inheritance in Interestingly, the role of Nup2 during mitotic NPC segregation is independent of its importin α- and Ran-binding domains but relies on a central targeting domain that is necessary for localization and viability. To test whether mitotic chromatin-associated Nup2 might function to bridge NPCs with chromatin during segregation, we provided an artificial link between NPCs and chromatin via Nup133 and histone H1. Using this approach, we bypassed the requirement of Nup2 for NPC segregation. This indicates that cells ensure accurate mitotic NPC segregation to daughter nuclei by linking mitotic DNA and NPC segregation via the mitotic specific chromatin association of Nup2.
[Mh] Termos MeSH primário: Aspergillus nidulans/metabolismo
Proteínas Fúngicas/metabolismo
Mitose
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Poro Nuclear/metabolismo
[Mh] Termos MeSH secundário: Aspergillus nidulans/genética
Aspergillus nidulans/crescimento & desenvolvimento
Cromatina/genética
Cromatina/metabolismo
DNA Fúngico/genética
DNA Fúngico/metabolismo
Proteínas Fúngicas/genética
Histonas/metabolismo
Microscopia de Fluorescência
Mutação
Poro Nuclear/genética
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Transdução de Sinais
Fatores de Tempo
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (DNA, Fungal); 0 (Fungal Proteins); 0 (Histones); 0 (Nuclear Pore Complex Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201610019


  8 / 33771 MEDLINE  
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[PMID]:29449480
[Au] Autor:Ghorani E; Quezada SA
[Ad] Endereço:Cancer Immunology Unit, Research Department of Haematology, University College London Cancer Institute, University College London, London, UK.
[Ti] Título:Chromatin regulation and immune escape.
[So] Source:Science;359(6377):745-746, 2018 02 16.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Cromatina
Evasão Tumoral/imunologia
[Mh] Termos MeSH secundário: Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Chromatin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180217
[St] Status:MEDLINE
[do] DOI:10.1126/science.aat0383


  9 / 33771 MEDLINE  
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[PMID]:29267285
[Au] Autor:Colombo DF; Burger L; Baubec T; Schübeler D
[Ad] Endereço:Friedrich Miescher Institute for Biomedical Research, Basel, Switzerland.
[Ti] Título:Binding of high mobility group A proteins to the mammalian genome occurs as a function of AT-content.
[So] Source:PLoS Genet;13(12):e1007102, 2017 12.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genomic location can inform on potential function and recruitment signals for chromatin-associated proteins. High mobility group (Hmg) proteins are of similar size as histones with Hmga1 and Hmga2 being particularly abundant in replicating normal tissues and in cancerous cells. While several roles for Hmga proteins have been proposed we lack a comprehensive description of their genomic location as a function of chromatin, DNA sequence and functional domains. Here we report such a characterization in mouse embryonic stem cells in which we introduce biotin-tagged constructs of wild-type and DNA-binding domain mutants. Comparative analysis of the genome-wide distribution of Hmga proteins reveals pervasive binding, a feature that critically depends on a functional DNA-binding domain and which is shared by both Hmga proteins. Assessment of the underlying queues instructive for this binding modality identifies AT richness, defined as high frequency of A or T bases, as the major criterion for local binding. Additionally, we show that other chromatin states such as those linked to cis-regulatory regions have little impact on Hmga binding both in stem and differentiated cells. As a consequence, Hmga proteins are preferentially found at AT-rich regions such as constitutively heterochromatic regions but are absent from enhancers and promoters arguing for a limited role in regulating individual genes. In line with this model, we show that genetic deletion of Hmga proteins in stem cells causes limited transcriptional effects and that binding is conserved in neuronal progenitors. Overall our comparative study describing the in vivo binding modality of Hmga1 and Hmga2 identifies the proteins' preference for AT-rich DNA genome-wide and argues against a suggested function of Hmga at regulatory regions. Instead we discover pervasive binding with enrichment at regions of higher AT content irrespective of local variation in chromatin modifications.
[Mh] Termos MeSH primário: Sequência Rica em At
Proteínas de Grupo de Alta Mobilidade/genética
Proteínas de Grupo de Alta Mobilidade/metabolismo
[Mh] Termos MeSH secundário: Animais
Composição de Bases
Sequência de Bases
Cromatina/genética
Cromatina/metabolismo
DNA/química
DNA/genética
DNA/metabolismo
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Células-Tronco Embrionárias/metabolismo
Histonas/genética
Camundongos
Camundongos Endogâmicos C57BL
Regiões Promotoras Genéticas
Ligação Proteica
Sequências Reguladoras de Ácido Nucleico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (DNA-Binding Proteins); 0 (High Mobility Group Proteins); 0 (Histones); 9007-49-2 (DNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171222
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007102


  10 / 33771 MEDLINE  
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[PMID]:28448742
[Au] Autor:Dabin J; Polo SE
[Ad] Endereço:a Epigenetics & Cell Fate Centre, UMR7216 CNRS , Paris Diderot University, Sorbonne Paris Cité , Paris , France.
[Ti] Título:Choreography of parental histones in damaged chromatin.
[So] Source:Nucleus;8(3):255-260, 2017 May 04.
[Is] ISSN:1949-1042
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the cell nucleus, DNA repair machineries operate on a chromatin substrate, whose integrity is key for preserving cell functions and identity. Yet, it is still unclear how the epigenetic information conveyed by chromatin is maintained during the DNA repair process. We recently characterized the dynamics of parental histones coupled to UV-C damage repair in human cells, providing insights into how the pre-damage chromatin state may be restored. Here, we summarize our main findings and discuss them in the context of epigenome maintenance following DNA damage. We further address the mechanistic aspects of repair-coupled histone dynamics and develop working hypotheses regarding their functional relevance in the cellular response to genotoxic stress.
[Mh] Termos MeSH primário: Cromatina/metabolismo
Histonas/metabolismo
[Mh] Termos MeSH secundário: Cromatina/efeitos da radiação
Reparo do DNA/efeitos da radiação
Epigenômica
Modelos Biológicos
Raios Ultravioleta/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1080/19491034.2017.1292192



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BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde