Base de dados : MEDLINE
Pesquisa : A11.284.430.106.279.345.190.160.180.270 [Categoria DeCS]
Referências encontradas : 627 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 63 ir para página                         

  1 / 627 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27771437
[Au] Autor:Carranza PG; Gargantini PR; Prucca CG; Torri A; Saura A; Svärd S; Lujan HD
[Ad] Endereço:Laboratorio de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Católica de Córdoba, Argentina.
[Ti] Título:Specific histone modifications play critical roles in the control of encystation and antigenic variation in the early-branching eukaryote Giardia lamblia.
[So] Source:Int J Biochem Cell Biol;81(Pt A):32-43, 2016 12.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:During evolution, parasitic microorganisms have faced the challenges of adapting to different environments to colonize a variety of hosts. Giardia lamblia, a common cause of intestinal disease, has developed fascinating strategies to adapt both outside and inside its host's intestine, such as trophozoite differentiation into cyst and the switching of its major surface antigens. How gene expression is regulated during these adaptive processes remains undefined. Giardia lacks some typical eukaryotic features, like canonical transcription factors, linker histone H1, and complex promoter regions; suggesting that post-transcriptional and translational control of gene expression is essential for parasite survival. However, epigenetic factors may also play critical roles at the transcriptional level. Here, we describe the most common post-translational histone modifications; characterize enzymes involved in these reactions, and analyze their association with the Giardia's differentiation processes. We present evidence that NAD -dependent and NAD -independent histone deacetylases regulate encystation; however, a unique NAD -independent histone deacetylase modulate antigenic switching. The rates of acetylation of H4K8 and H4K16 are critical for encystation, whereas a decrease in acetylation of H4K8 and methylation of H3K9 occur preferentially during antigenic variation. These results show the complexity of the mechanisms regulating gene expression in this minimalistic protozoan parasite.
[Mh] Termos MeSH primário: Variação Antigênica
Giardia lamblia/imunologia
Giardia lamblia/metabolismo
Histonas/metabolismo
[Mh] Termos MeSH secundário: Acetilação/efeitos dos fármacos
Variação Antigênica/efeitos dos fármacos
Eucromatina/metabolismo
Giardia lamblia/citologia
Giardia lamblia/genética
Heterocromatina/metabolismo
Inibidores de Histona Desacetilases/farmacologia
Histona Desacetilases/metabolismo
Histonas/química
Lisina/metabolismo
NAD/metabolismo
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Euchromatin); 0 (Heterochromatin); 0 (Histone Deacetylase Inhibitors); 0 (Histones); 0U46U6E8UK (NAD); EC 3.5.1.98 (Histone Deacetylases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171217
[Lr] Data última revisão:
171217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161106
[St] Status:MEDLINE


  2 / 627 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28807902
[Au] Autor:Li Y; Wang C; Cai W; Sengupta S; Zavortink M; Deng H; Girton J; Johansen J; Johansen KM
[Ad] Endereço:Roy J. Carver Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA.
[Ti] Título:H2Av facilitates H3S10 phosphorylation but is not required for heat shock-induced chromatin decondensation or transcriptional elongation.
[So] Source:Development;144(18):3232-3240, 2017 09 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A model has been proposed in which JIL-1 kinase-mediated H3S10 and H2Av phosphorylation is required for transcriptional elongation and heat shock-induced chromatin decondensation. However, here we show that although H3S10 phosphorylation is indeed compromised in the null mutant, chromatin decondensation at heat shock loci is unaffected in the absence of JIL-1 as well as of H2Av and that there is no discernable decrease in the elongating form of RNA polymerase II in either mutant. Furthermore, mRNA for the major heat shock protein Hsp70 is transcribed at robust levels in both and null mutants. Using a different chromatin remodeling paradigm that is JIL-1 dependent, we provide evidence that ectopic tethering of JIL-1 and subsequent H3S10 phosphorylation recruits PARP-1 to the remodeling site independently of H2Av phosphorylation. These data strongly suggest that H2Av or H3S10 phosphorylation by JIL-1 is not required for chromatin decondensation or transcriptional elongation in .
[Mh] Termos MeSH primário: Cromatina/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/metabolismo
Histonas/metabolismo
Fosfosserina/metabolismo
Elongação da Transcrição Genética
[Mh] Termos MeSH secundário: Animais
Eucromatina/metabolismo
Proteínas de Fluorescência Verde/metabolismo
Resposta ao Choque Térmico/genética
Immunoblotting
Imuno-Histoquímica
Óperon Lac/genética
Mutação/genética
Fosforilação
Poli(ADP-Ribose) Polimerases/metabolismo
Cromossomos Politênicos/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Transgenes
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Chromatin); 0 (Drosophila Proteins); 0 (Euchromatin); 0 (H2AV protein, Drosophila); 0 (Histones); 147336-22-9 (Green Fluorescent Proteins); 17885-08-4 (Phosphoserine); EC 2.4.2.30 (Poly(ADP-ribose) Polymerases); EC 2.7.11.1 (JIL-1 protein, Drosophila); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE
[do] DOI:10.1242/dev.151134


  3 / 627 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28735899
[Au] Autor:Xue Y; Pradhan SK; Sun F; Chronis C; Tran N; Su T; Van C; Vashisht A; Wohlschlegel J; Peterson CL; Timmers HTM; Kurdistani SK; Carey MF
[Ad] Endereço:Department of Biological Chemistry, David Geffen School of Medicine, UCLA, Los Angeles, CA 90095, USA.
[Ti] Título:Mot1, Ino80C, and NC2 Function Coordinately to Regulate Pervasive Transcription in Yeast and Mammals.
[So] Source:Mol Cell;67(4):594-607.e4, 2017 Aug 17.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pervasive transcription initiates from cryptic promoters and is observed in eukaryotes ranging from yeast to mammals. The Set2-Rpd3 regulatory system prevents cryptic promoter function within expressed genes. However, conserved systems that control pervasive transcription within intergenic regions have not been well established. Here we show that Mot1, Ino80 chromatin remodeling complex (Ino80C), and NC2 co-localize on chromatin and coordinately suppress pervasive transcription in S. cerevisiae and murine embryonic stem cells (mESCs). In yeast, all three proteins bind subtelomeric heterochromatin through a Sir3-stimulated mechanism and to euchromatin via a TBP-stimulated mechanism. In mESCs, the proteins bind to active and poised TBP-bound promoters along with promoters of polycomb-silenced genes apparently lacking TBP. Depletion of Mot1, Ino80C, or NC2 by anchor away in yeast or RNAi in mESCs leads to near-identical transcriptome phenotypes, with new subtelomeric transcription in yeast, and greatly increased pervasive transcription in both yeast and mESCs.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/metabolismo
Células-Tronco Embrionárias/enzimologia
Fosfoproteínas/metabolismo
Proteínas Repressoras/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
Fatores Associados à Proteína de Ligação a TATA/metabolismo
Fatores de Transcrição/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Sítios de Ligação
Linhagem Celular
Eucromatina/genética
Eucromatina/metabolismo
Regulação Fúngica da Expressão Gênica
Inativação Gênica
Genótipo
Heterocromatina/genética
Heterocromatina/metabolismo
Fenótipo
Fosfoproteínas/genética
Regiões Promotoras Genéticas
Ligação Proteica
Interferência de RNA
Proteínas Repressoras/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas Reguladoras de Informação Silenciosa de Saccharomyces cerevisiae/genética
Proteínas Reguladoras de Informação Silenciosa de Saccharomyces cerevisiae/metabolismo
Fatores Associados à Proteína de Ligação a TATA/genética
Proteína de Ligação a TATA-Box/genética
Proteína de Ligação a TATA-Box/metabolismo
Fatores de Transcrição/genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BUR6 protein, S cerevisiae); 0 (Euchromatin); 0 (Heterochromatin); 0 (INO80 complex, S cerevisiae); 0 (Phosphoproteins); 0 (Repressor Proteins); 0 (SIR3 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Silent Information Regulator Proteins, Saccharomyces cerevisiae); 0 (TATA-Binding Protein Associated Factors); 0 (TATA-Box Binding Protein); 0 (Transcription Factors); 0 (down-regulator of transcription 1); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (BTAF1 protein, mouse); EC 3.6.1.- (INO80 protein, mouse); EC 3.6.1.- (MOT1 protein, S cerevisiae)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE


  4 / 627 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28648780
[Au] Autor:Flury V; Georgescu PR; Iesmantavicius V; Shimada Y; Kuzdere T; Braun S; Bühler M
[Ad] Endereço:Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, 4058 Basel, Switzerland; University of Basel, Petersplatz 10, 4003 Basel, Switzerland.
[Ti] Título:The Histone Acetyltransferase Mst2 Protects Active Chromatin from Epigenetic Silencing by Acetylating the Ubiquitin Ligase Brl1.
[So] Source:Mol Cell;67(2):294-307.e9, 2017 Jul 20.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Faithful propagation of functionally distinct chromatin states is crucial for maintaining cellular identity, and its breakdown can lead to diseases such as cancer. Whereas mechanisms that sustain repressed states have been intensely studied, regulatory circuits that protect active chromatin from inactivating signals are not well understood. Here we report a positive feedback loop that preserves the transcription-competent state of RNA polymerase II-transcribed genes. We found that Pdp3 recruits the histone acetyltransferase Mst2 to H3K36me3-marked chromatin. Thereby, Mst2 binds to all transcriptionally active regions genome-wide. Besides acetylating histone H3K14, Mst2 also acetylates Brl1, a component of the histone H2B ubiquitin ligase complex. Brl1 acetylation increases histone H2B ubiquitination, which positively feeds back on transcription and prevents ectopic heterochromatin assembly. Our work uncovers a molecular pathway that secures epigenome integrity and highlights the importance of opposing feedback loops for the partitioning of chromatin into transcriptionally active and inactive states.
[Mh] Termos MeSH primário: Montagem e Desmontagem da Cromatina
Eucromatina/enzimologia
Inativação Gênica
Histona Acetiltransferases/metabolismo
Histonas/metabolismo
Proteínas de Membrana/metabolismo
Proteínas Nucleares/metabolismo
Processamento de Proteína Pós-Traducional
Proteínas de Schizosaccharomyces pombe/metabolismo
Schizosaccharomyces/enzimologia
[Mh] Termos MeSH secundário: Acetilação
Eucromatina/genética
Retroalimentação Fisiológica
Regulação Fúngica da Expressão Gênica
Heterocromatina/enzimologia
Heterocromatina/genética
Histona Acetiltransferases/genética
Proteínas de Membrana/genética
Mutação
Proteínas Nucleares/genética
Schizosaccharomyces/genética
Proteínas de Schizosaccharomyces pombe/genética
Transcrição Genética
Ativação Transcricional
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Brr6 protein, S pombe); 0 (Euchromatin); 0 (Heterochromatin); 0 (Histones); 0 (Membrane Proteins); 0 (Nuclear Proteins); 0 (Schizosaccharomyces pombe Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Mst2 protein, S pombe)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE


  5 / 627 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28330620
[Au] Autor:Rahjouei A; Pirouz M; Di Virgilio M; Kamin D; Kessel M
[Ad] Endereço:RG Developmental Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg, 37077 Göttingen, Germany; DNA Repair and Maintenance of Genome Stability, Max-Delbruck Center for Molecular Medicine, 13125 Berlin-Buch, Germany.
[Ti] Título:MAD2L2 Promotes Open Chromatin in Embryonic Stem Cells and Derepresses the Dppa3 Locus.
[So] Source:Stem Cell Reports;8(4):813-821, 2017 Apr 11.
[Is] ISSN:2213-6711
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The chromatin of naive embryonic stem cells (ESCs) has a largely open configuration, as evident by the lack of condensed heterochromatin and the hypomethylation of DNA. Several molecular mechanisms promoting this constellation were previously identified. Here we present evidence for an important epigenetic function of MAD2L2, a protein originally known for its role in DNA damage repair, and for its requirement in germ cell development. We demonstrate using super-resolution microscopy that numerous MAD2L2 microfoci are exclusively associated with euchromatin, similar to other factors of the DNA damage response. In the absence of MAD2L2 the amount of heterochromatin demarcated by H3K9me2 was significantly increased. Among the most strongly suppressed genes was Dppa3, an ESC- and germ-cell-specific gene regulating DNA methylation. In Mad2l2-deficient ESCs 5-methylcytosine levels were globally increased, while several imprinted genes became hypomethylated and transcriptionally activated. Our results emphasize the important function of MAD2L2 for the open chromatin configuration of ESCs.
[Mh] Termos MeSH primário: Epigênese Genética
Eucromatina/metabolismo
Proteínas Mad2/metabolismo
Células-Tronco Embrionárias Murinas/citologia
Proteínas Repressoras/genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Dano ao DNA
Metilação de DNA
Regulação para Baixo
Eucromatina/genética
Deleção de Genes
Loci Gênicos
Heterocromatina/genética
Heterocromatina/metabolismo
Proteínas Mad2/análise
Proteínas Mad2/genética
Camundongos
Células-Tronco Embrionárias Murinas/metabolismo
Ativação Transcricional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dppa3 protein, mouse); 0 (Euchromatin); 0 (Heterochromatin); 0 (Mad2 Proteins); 0 (Mad2l2 protein, mouse); 0 (Repressor Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE


  6 / 627 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28320872
[Au] Autor:Fromental-Ramain C; Ramain P; Hamiche A
[Ad] Endereço:Département de Génomique Fonctionnelle et Cancer, Institut de Génétique et Biologie Moléculaire et Cellulaire, UdS, CNRS, INSERM, Equipe Labélisée Ligue contre le Cancer, Illkirch, France.
[Ti] Título:The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3 Deposition and Heterochromatin Formation.
[So] Source:Mol Cell Biol;37(12), 2017 Jun 15.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histone variants are nonallelic isoforms of canonical histones, and they are deposited, in contrast to canonical histones, in a replication-independent (RI) manner. RI deposition of H3.3, a histone variant from the H3.3 family, is mediated in mammals by distinct pathways involving either the histone regulator A (HIRA) complex or the death-associated protein (DAXX)/α-thalassemia X-linked mental retardation protein (ATRX) complex. Here, we investigated the function of the DAXX-like protein (DLP) by using both fly genetic approaches and protein biochemistry. DLP specifically interacts with H3.3 and shows a prominent localization on the base of the X chromosome, where it appears to act in concert with XNP, the homolog of ATRX, in heterochromatin assembly and maintenance. The functional association between DLP and XNP is further supported by a series of experiments that illustrate genetic interactions and the DLP-XNP-dependent localization of specific chromosomal proteins. In addition, DLP both participates in the RI deposition of H3.3 and associates with anti-silencing factor 1 (ASF1). We suggest, in agreement with a recently proposed model, that DLP and ASF1 are part of a predeposition complex, which is recruited by XNP and is necessary to prevent DNA exposure in the nucleus.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Proteínas de Ciclo Celular/metabolismo
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/metabolismo
Heterocromatina/metabolismo
Histonas/metabolismo
Proteínas Nucleares/metabolismo
[Mh] Termos MeSH secundário: Animais
Cromossomos/metabolismo
DNA Helicases/metabolismo
Replicação do DNA
Drosophila melanogaster/embriologia
Embrião não Mamífero/metabolismo
Epistasia Genética
Eucromatina/metabolismo
Feminino
Masculino
Modelos Biológicos
Mutação/genética
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cell Cycle Proteins); 0 (Daxx-like protein, Drosophila); 0 (Drosophila Proteins); 0 (Euchromatin); 0 (Heterochromatin); 0 (Histones); 0 (Nuclear Proteins); 0 (asf1 protein, Drosophila); EC 3.6.1.- (XNP protein, Drosophila); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE


  7 / 627 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28235841
[Au] Autor:Kheir E; Krude T
[Ad] Endereço:Department of Zoology, University of Cambridge, Downing Street, Cambridge CB2 3EJ, UK.
[Ti] Título:Non-coding Y RNAs associate with early replicating euchromatin in concordance with the origin recognition complex.
[So] Source:J Cell Sci;130(7):1239-1250, 2017 Apr 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Non-coding Y RNAs are essential for the initiation of chromosomal DNA replication in vertebrates, yet their association with chromatin during the cell cycle is not characterised. Here, we quantify human Y RNA levels in soluble and chromatin-associated intracellular fractions and investigate, topographically, their dynamic association with chromatin during the cell cycle. We find that, on average, about a million Y RNA molecules are present in the soluble fraction of a proliferating cell, and 5-10-fold less are in association with chromatin. These levels decrease substantially during quiescence. No significant differences are apparent between cancer and non-cancer cell lines. Y RNAs associate with euchromatin throughout the cell cycle. Their levels are 2-4-fold higher in S phase than in G1 phase or mitosis. Y RNAs are not detectable at active DNA replication foci, and re-associate with replicated euchromatin during mid and late S phase. The dynamics and sites of Y1 RNA association with chromatin are in concordance with those of the origin recognition complex (ORC). Our data therefore suggest a functional role of Y RNAs in a common pathway with ORC.
[Mh] Termos MeSH primário: Replicação do DNA/genética
Eucromatina/metabolismo
Complexo de Reconhecimento de Origem/genética
RNA não Traduzido/genética
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Proliferação Celular
Fase G1
Seres Humanos
Neoplasias/genética
Neoplasias/patologia
Fase S
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Euchromatin); 0 (Origin Recognition Complex); 0 (RNA, Untranslated)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170226
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.197566


  8 / 627 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28212747
[Au] Autor:Liu Z; Kraus WL
[Ad] Endereço:The Laboratory of Signaling and Gene Expression, Cecil H. and Ida Green Center for Reproductive Biology Sciences and The Division of Basic Research, Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center, Dallas, TX 75390-8511, USA; Program in Genetics, Development, and Disease, Graduate School of Biomedical Sciences, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
[Ti] Título:Catalytic-Independent Functions of PARP-1 Determine Sox2 Pioneer Activity at Intractable Genomic Loci.
[So] Source:Mol Cell;65(4):589-603.e9, 2017 Feb 16.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pioneer transcription factors (TFs) function as genomic first responders, binding to inaccessible regions of chromatin to promote enhancer formation. The mechanism by which pioneer TFs gain access to chromatin remains an important unanswered question. Here we show that PARP-1, a nucleosome-binding protein, cooperates with intrinsic properties of the pioneer TF Sox2 to facilitate its binding to intractable genomic loci in embryonic stem cells. These actions of PARP-1 occur independently of its poly(ADP-ribosyl) transferase activity. PARP-1-dependent Sox2-binding sites reside in euchromatic regions of the genome with relatively high nucleosome occupancy and low co-occupancy by other transcription factors. PARP-1 stabilizes Sox2 binding to nucleosomes at suboptimal sites through cooperative interactions on DNA. Our results define intrinsic and extrinsic features that determine Sox2 pioneer activity. The conditional pioneer activity observed with Sox2 at a subset of binding sites may be a key feature of other pioneer TFs operating at intractable genomic loci.
[Mh] Termos MeSH primário: DNA/metabolismo
Células-Tronco Embrionárias/enzimologia
Eucromatina/enzimologia
Regulação da Expressão Gênica no Desenvolvimento
Loci Gênicos
Nucleossomos/enzimologia
Células-Tronco Pluripotentes/enzimologia
Poli(ADP-Ribose) Polimerase-1/metabolismo
Fatores de Transcrição SOXB1/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Linhagem Celular
DNA/genética
Eucromatina/genética
Seres Humanos
Camundongos
Nucleossomos/genética
Poli(ADP-Ribose) Polimerase-1/genética
Ligação Proteica
Fatores de Transcrição SOXB1/genética
Transdução de Sinais
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Euchromatin); 0 (Nucleosomes); 0 (SOX2 protein, human); 0 (SOXB1 Transcription Factors); 0 (Sox2 protein, mouse); 9007-49-2 (DNA); EC 2.4.2.30 (PARP1 protein, human); EC 2.4.2.30 (Parp1 protein, mouse); EC 2.4.2.30 (Poly (ADP-Ribose) Polymerase-1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170219
[St] Status:MEDLINE


  9 / 627 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28148649
[Au] Autor:Shakyawar DK; Dayma K; Ramadhas A; Varalakshmi C; Radha V
[Ad] Endereço:Centre for Cellular and Molecular Biology, Hyderabad 500 007, India.
[Ti] Título:C3G shows regulated nucleocytoplasmic exchange and represses histone modifications associated with euchromatin.
[So] Source:Mol Biol Cell;28(7):984-995, 2017 Apr 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:C3G (RapGEF1) is a ubiquitously expressed guanine nucleotide exchange factor that functions in signaling pathways regulating cell proliferation, apoptosis, and actin reorganization. It is essential for differentiation and early embryonic development in mice. Overexpressed C3G shows predominant cytoplasmic localization, but endogenous C3G is a component of nuclear fractions in a variety of cell types. Coexpression of importin-α and inhibition of nuclear export by leptomycin B resulted in predominant nuclear localization of C3G. Functional NLSs, NES, and GSK3-ß-dependent phosphorylation regulate its dynamic nuclear localization. C3G translocates to the nucleus in response to myogenic differentiation and sublethal dose of cisplatin. C3G is associated with chromatin and nuclear matrix fractions. Cells with C3G localized in the nucleus showed peripheralization of heterochromatin and reduced histone modifications associated with euchromatin. Short hairpin RNA-mediated depletion of C3G in epithelial cells resulted in reduced expression of CDK inhibitors and the histone demethylase KDM5A. Myoblast clones with CRISPR/Cas9-mediated knockout of C3G failed to show repression of histone marks and did not show up-regulation of myosin heavy chain and myotube formation when grown in differentiation medium. Our results document regulated nucleocytoplasmic exchange of C3G in response to physiological stimuli and provide insights into nuclear functions for C3G.
[Mh] Termos MeSH primário: Eucromatina/fisiologia
Fator 2 de Liberação do Nucleotídeo Guanina/metabolismo
Fator 2 de Liberação do Nucleotídeo Guanina/fisiologia
Código das Histonas/fisiologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Transporte Ativo do Núcleo Celular/fisiologia
Animais
Diferenciação Celular
Linhagem Celular Tumoral
Núcleo Celular/metabolismo
Proliferação Celular
Eucromatina/metabolismo
Ácidos Graxos Insaturados/metabolismo
Quinase 3 da Glicogênio Sintase/metabolismo
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Fator 2 de Liberação do Nucleotídeo Guanina/genética
Camundongos
Desenvolvimento Muscular
Sinais de Localização Nuclear
Fosforilação
Transdução de Sinais
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Euchromatin); 0 (Fatty Acids, Unsaturated); 0 (Guanine Nucleotide Exchange Factors); 0 (Guanine Nucleotide-Releasing Factor 2); 0 (Nuclear Localization Signals); EC 2.7.11.26 (Glycogen Synthase Kinase 3); Y031I2N1EO (leptomycin B)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170203
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-09-0660


  10 / 627 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28057760
[Au] Autor:Stephens AD; Banigan EJ; Adam SA; Goldman RD; Marko JF
[Ad] Endereço:Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208 andrew.stephens@northwestern.edu.
[Ti] Título:Chromatin and lamin A determine two different mechanical response regimes of the cell nucleus.
[So] Source:Mol Biol Cell;28(14):1984-1996, 2017 Jul 07.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cell nucleus must continually resist and respond to intercellular and intracellular mechanical forces to transduce mechanical signals and maintain proper genome organization and expression. Altered nuclear mechanics is associated with many human diseases, including heart disease, progeria, and cancer. Chromatin and nuclear envelope A-type lamin proteins are known to be key nuclear mechanical components perturbed in these diseases, but their distinct mechanical contributions are not known. Here we directly establish the separate roles of chromatin and lamin A/C and show that they determine two distinct mechanical regimes via micromanipulation of single isolated nuclei. Chromatin governs response to small extensions (<3 µm), and euchromatin/heterochromatin levels modulate the stiffness. In contrast, lamin A/C levels control nuclear strain stiffening at large extensions. These results can be understood through simulations of a polymeric shell and cross-linked polymer interior. Our results provide a framework for understanding the differential effects of chromatin and lamin A/C in cell nuclear mechanics and their alterations in disease.
[Mh] Termos MeSH primário: Núcleo Celular/fisiologia
Cromatina/fisiologia
Lamina Tipo A/fisiologia
[Mh] Termos MeSH secundário: Técnicas de Cultura de Células
Cromatina/metabolismo
Eucromatina/fisiologia
Heterocromatina/fisiologia
Seres Humanos
Lamina Tipo A/metabolismo
Mecanotransdução Celular/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Euchromatin); 0 (Heterochromatin); 0 (Lamin Type A)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-09-0653



página 1 de 63 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

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