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Pesquisa : G02.111.035.538 [Categoria DeCS]
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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


  2 / 27657 MEDLINE  
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[PMID]:29287247
[Au] Autor:Beloborodov SS; Bao J; Krylova SM; Shala-Lawrence A; Johnson PE; Krylov SN
[Ad] Endereço:Department of Chemistry and Centre for Research on Biomolecular Interactions, York University, Toronto, Ontario M3J 1P3, Canada.
[Ti] Título:Aptamer facilitated purification of functional proteins.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1073:201-206, 2018 Jan 15.
[Is] ISSN:1873-376X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:DNA aptamers are attractive capture probes for affinity chromatography since, in contrast to antibodies, they can be chemically synthesized and, in contrast to tag-specific capture probes (such as Nickel-NTA or Glutathione), they can be used for purification of proteins free of genetic modifications (such as His or GST tags). Despite these attractive features of aptamers as capture probes, there are only a few reports on aptamer-based protein purification and none of them includes a test of the purified protein's activity, thus, leaving discouraging doubts about method's ability to purify proteins in their active state. The goal of this work was to prove that aptamers could facilitate isolation of active proteins. We refined a complete aptamer-based affinity purification procedure, which takes 4 h to complete. We further applied this procedure to purify two recombinant proteins, MutS and AlkB, from bacterial cell culture: 0.21 mg of 85%-pure AlkB from 4 mL of culture and 0.24 mg of 82%-pure MutS from 0.5 mL of culture. Finally, we proved protein activity by two capillary electrophoresis based assays: an enzymatic assay for AlkB and a DNA-binding assay for MutS. We suggest that in combination with aptamer selection for non-purified protein targets in crude cell lysate, aptamer-based purification provides a means of fast isolation of tag-free recombinant proteins in their native state without the use of antibodies.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/química
Cromatografia de Afinidade/métodos
Ácidos Nucleicos Imobilizados/química
Proteínas Recombinantes/isolamento & purificação
[Mh] Termos MeSH secundário: Enzimas AlkB/química
Enzimas AlkB/genética
Enzimas AlkB/isolamento & purificação
Enzimas AlkB/metabolismo
Aptâmeros de Nucleotídeos/metabolismo
Eletroforese Capilar
Eletroforese em Gel de Poliacrilamida
Escherichia coli/genética
Ácidos Nucleicos Imobilizados/metabolismo
Metilação
Proteína MutS de Ligação de DNA com Erro de Pareamento/química
Proteína MutS de Ligação de DNA com Erro de Pareamento/genética
Proteína MutS de Ligação de DNA com Erro de Pareamento/isolamento & purificação
Proteína MutS de Ligação de DNA com Erro de Pareamento/metabolismo
Ligação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aptamers, Nucleotide); 0 (Immobilized Nucleic Acids); 0 (Recombinant Proteins); EC 1.14.11.33 (AlkB Enzymes); EC 3.6.1.3 (MutS DNA Mismatch-Binding Protein)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE


  3 / 27657 MEDLINE  
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[PMID]:29253878
[Au] Autor:Asam K; Staniszewski A; Zhang H; Melideo SL; Mazzeo A; Voronkov M; Huber KL; Pérez E; Stock M; Stock JB; Arancio O; Nicholls RE
[Ad] Endereço:Department of Pathology and Cell Biology, Columbia University, New York, NY, United States of America.
[Ti] Título:Eicosanoyl-5-hydroxytryptamide (EHT) prevents Alzheimer's disease-related cognitive and electrophysiological impairments in mice exposed to elevated concentrations of oligomeric beta-amyloid.
[So] Source:PLoS One;12(12):e0189413, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Soluble forms of oligomeric beta-amyloid (Aß) are thought to play a central role in Alzheimer's disease (AD). Transgenic manipulation of methylation of the serine/threonine protein phosphatase, PP2A, was recently shown to alter the sensitivity of mice to AD-related impairments resulting from acute exposure to elevated levels of Aß. In addition, eicosanoyl-5-hydroxytryptamide (EHT), a naturally occurring component from coffee beans that modulates PP2A methylation, was shown to confer therapeutic benefits in rodent models of AD and Parkinson's disease. Here, we tested the hypothesis that EHT protects animals from the pathological effects of exposure to elevated levels of soluble oligomeric Aß. We treated mice with EHT-containing food at two different doses and assessed the sensitivity of these animals to Aß-induced behavioral and electrophysiological impairments. We found that EHT administration protected animals from Aß-induced cognitive impairments in both a radial-arm water maze and contextual fear conditioning task. We also found that both chronic and acute EHT administration prevented Aß-induced impairments in long-term potentiation. These data add to the accumulating evidence suggesting that interventions with pharmacological agents, such as EHT, that target PP2A activity may be therapeutically beneficial for AD and other neurological conditions.
[Mh] Termos MeSH primário: Doença de Alzheimer/tratamento farmacológico
Peptídeos beta-Amiloides/química
Transtornos Cognitivos/prevenção & controle
Serotonina/análogos & derivados
[Mh] Termos MeSH secundário: Doença de Alzheimer/patologia
Animais
Café
Cognição/efeitos dos fármacos
Condicionamento (Psicologia)
Modelos Animais de Doenças
Eletrofisiologia
Medo
Feminino
Potenciação de Longa Duração
Masculino
Aprendizagem em Labirinto
Metilação
Camundongos
Camundongos Endogâmicos C57BL
Doenças do Sistema Nervoso/tratamento farmacológico
Doenças do Sistema Nervoso/patologia
Plasticidade Neuronal
Fosforilação
Serotonina/farmacologia
Solubilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Peptides); 0 (Coffee); 0 (eicosanoyl-5-hydroxytryptamide); 333DO1RDJY (Serotonin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171219
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189413


  4 / 27657 MEDLINE  
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[PMID]:29307522
[Au] Autor:Riberio DF; Cella PS; da Silva LECM; Jordao AA; Deminice R
[Ad] Endereço:Department of Physical Education, State University of Londrina, Londrina, PR, Brazil.
[Ti] Título:Acute exercise alters homocysteine plasma concentration in an intensity-dependent manner due increased methyl flux in liver of rats.
[So] Source:Life Sci;196:63-68, 2018 Mar 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:PURPOSE: We aimed to determine the effects of different intensities of acute exercise on Hcy plasma levels, and the exercise-induced changes in Hcy liver metabolism. METHOD: First, thirty-two Wistar rats were randomly submitted to an acute bout of swimming exercise carrying a load of 2% (n=8), 4% (n=8) and 6% (n=8) of their total body weight attached in their tail. Control rats remained rested (n=8). Blood samples were taken from tail vein for plasma S-containing amino acids determination before (Rest) and post, 1, 2, 3, 4, 6, and 10h after acute swimming exercise. Second, 56 exercised rats (4% loads) were euthanized before (Rest) and1, 2, 3, 4, 6, and 10h after acute swimming exercise. Blood and liver samples were collected for amino acids and keys genes involved in the Hcy metabolism assay. RESULTS: Acute exercise increases (P<0.05) plasma Hcy concentration in an intensity-dependent manner (rest 7.7±0.8; 6% load 13.8±3.6; 4% load 12.2±2.9±and 2% load 10.1±2.6, µmol/L); this increase is transient and does not promote hyperhomocysteinemia (<15µmol/L).Exercise-induced increased plasma Hcywas accompanied by the decreased liver S-adenosylmethionine/S-adenosylhomocysteine ratio and elevated MAT1a mRNA content. Acute exercise also caused elevated mRNA of key enzymes of transsulfuration (CBS) and remethylation (BHMT and the MTRR). CONCLUSION: Our data provided evidence that acute exercise increases plasma Hcy concentration due to the augmented requirement for methylated compounds that increases liver SAM consumption. Also, Hcy remethylation and transsulfuration are coordinately regulated to maintain methyl balance.
[Mh] Termos MeSH primário: Homocisteína/sangue
Fígado/metabolismo
Condicionamento Físico Animal/fisiologia
[Mh] Termos MeSH secundário: Animais
Peso Corporal/efeitos dos fármacos
Hiper-Homocisteinemia/metabolismo
Masculino
Metionina Adenosiltransferase/metabolismo
Metilação
Ratos
Ratos Wistar
S-Adenosil-Homocisteína/metabolismo
S-Adenosilmetionina/metabolismo
Natação/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0LVT1QZ0BA (Homocysteine); 7LP2MPO46S (S-Adenosylmethionine); 979-92-0 (S-Adenosylhomocysteine); EC 2.5.1.6 (Mat1a protein, rat); EC 2.5.1.6 (Methionine Adenosyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


  5 / 27657 MEDLINE  
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[PMID]:28450737
[Au] Autor:Hyun K; Jeon J; Park K; Kim J
[Ad] Endereço:Laboratory of Eukaryotic Transcription, Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon, South Korea.
[Ti] Título:Writing, erasing and reading histone lysine methylations.
[So] Source:Exp Mol Med;49(4):e324, 2017 04 28.
[Is] ISSN:2092-6413
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histone modifications are key epigenetic regulatory features that have important roles in many cellular events. Lysine methylations mark various sites on the tail and globular domains of histones and their levels are precisely balanced by the action of methyltransferases ('writers') and demethylases ('erasers'). In addition, distinct effector proteins ('readers') recognize specific methyl-lysines in a manner that depends on the neighboring amino-acid sequence and methylation state. Misregulation of histone lysine methylation has been implicated in several cancers and developmental defects. Therefore, histone lysine methylation has been considered a potential therapeutic target, and clinical trials of several inhibitors of this process have shown promising results. A more detailed understanding of histone lysine methylation is necessary for elucidating complex biological processes and, ultimately, for developing and improving disease treatments. This review summarizes enzymes responsible for histone lysine methylation and demethylation and how histone lysine methylation contributes to various biological processes.
[Mh] Termos MeSH primário: Código das Histonas
Histona Desmetilases/metabolismo
Histona-Lisina N-Metiltransferase/metabolismo
Histonas/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Animais
Seres Humanos
Metilação
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histones); EC 1.14.11.- (Histone Demethylases); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180224
[Lr] Data última revisão:
180224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1038/emm.2017.11


  6 / 27657 MEDLINE  
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[PMID]:28450734
[Au] Autor:Woo H; Dam Ha S; Lee SB; Buratowski S; Kim T
[Ad] Endereço:Department of Life Science, Ewha Womans University, Seoul, Korea.
[Ti] Título:Modulation of gene expression dynamics by co-transcriptional histone methylations.
[So] Source:Exp Mol Med;49(4):e326, 2017 04 28.
[Is] ISSN:2092-6413
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Co-transcriptional methylations of histone H3 at lysines 4 and 36, highly conserved methyl marks from yeast to humans, have profound roles in regulation of histone acetylation. These modifications function to recruit and/or activate distinct histone acetyltransferases (HATs) or histone deacetylases (HDACs). Whereas H3K4me3 increases acetylation at promoters via multiple HATs, H3K4me2 targets Set3 HDAC to deacetylate histones in 5' transcribed regions. In 3' regions of genes, H3K36me2/3 facilitates deacetylation by Rpd3S HDAC and slows elongation. Despite their important functions in deacetylation, no strong effects on global gene expression have been seen under optimized or laboratory growth conditions. Instead, H3K4me2-Set3 HDAC and Set2-Rpd3S pathways primarily delay the kinetics of messenger RNA (mRNA) and long noncoding RNA (lncRNA) induction upon environmental changes. A majority of mRNA genes regulated by these pathways have an overlapping lncRNA transcription either from an upstream or an antisense promoter. Surprisingly, the distance between mRNA and lncRNA promoters seems to specify the repressive effects of the two pathways. Given that co-transcriptional methylations and acetylation have been linked to many cancers, studying their functions in a dynamic condition or during cancer progression will be much more important and help identify novel genes associated with cancers.
[Mh] Termos MeSH primário: Histonas/metabolismo
Processamento de Proteína Pós-Traducional
Ativação Transcricional
[Mh] Termos MeSH secundário: Acetilação
Animais
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Metilação
RNA Longo não Codificante/genética
RNA Longo não Codificante/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histones); 0 (RNA, Long Noncoding); 0 (RNA, Messenger)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180224
[Lr] Data última revisão:
180224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1038/emm.2017.19


  7 / 27657 MEDLINE  
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[PMID]:29248353
[Au] Autor:Matthiesen RA; Varney ML; Xu PC; Rier AS; Wiemer DF; Holstein SA
[Ad] Endereço:Department of Chemistry, University of Iowa, Iowa City, IA 52242-1294, United States.
[Ti] Título:α-Methylation enhances the potency of isoprenoid triazole bisphosphonates as geranylgeranyl diphosphate synthase inhibitors.
[So] Source:Bioorg Med Chem;26(2):376-385, 2018 01 15.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Disruption of protein geranylgeranylation via inhibition of geranylgeranyl diphosphate synthase (GGDPS) represents a novel therapeutic strategy for a variety of malignancies, especially those characterized by excessive protein secretion such as multiple myeloma. Our work has demonstrated that some isoprenoid triazole bisphosphonates are potent and selective inhibitors of GGDPS. Here we present the synthesis and biological evaluation of a new series of isoprenoid triazoles modified by incorporation of a methyl group at the α-carbon. These studies reveal that incorporation of an α-methyl substituent enhances the potency of these compounds as GGDPS inhibitors, and, in the case of the homogeranyl/homoneryl series, abrogates the effects of olefin stereochemistry on inhibitory activity. The incorporation of the methyl group allowed preparation of a POM-prodrug, which displayed a 10-fold increase in cellular activity compared to the corresponding salt. These studies form the basis for future preclinical studies investigating the anti-myeloma activity of these novel α-methyl triazole bisphosphonates.
[Mh] Termos MeSH primário: Difosfonatos/farmacologia
Inibidores Enzimáticos/farmacologia
Farnesiltranstransferase/antagonistas & inibidores
Terpenos/farmacologia
Triazóis/farmacologia
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Difosfonatos/síntese química
Difosfonatos/química
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Farnesiltranstransferase/metabolismo
Seres Humanos
Metilação
Estrutura Molecular
Relação Estrutura-Atividade
Terpenos/síntese química
Terpenos/química
Triazóis/síntese química
Triazóis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Diphosphonates); 0 (Enzyme Inhibitors); 0 (Terpenes); 0 (Triazoles); EC 2.5.1.29 (Farnesyltranstransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171218
[St] Status:MEDLINE


  8 / 27657 MEDLINE  
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[PMID]:28456971
[Au] Autor:Aoshima K; Kimura T; Okada Y
[Ad] Endereço:Laboratory of Comparative Pathology, Graduate School of Veterinary Medicine, Hokkaido University, N18W9, Kita-ku, Sapporo, 060-0818, Japan.
[Ti] Título:Use of Histone K-M Mutants for the Analysis of Transcriptional Regulation in Mouse Zygotes.
[So] Source:Methods Mol Biol;1605:259-270, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histone modifications are dramatically altered during the pronuclear (PN) stage of zygotes, and more markedly in paternal than maternal pronuclei. Among various types of histone modifications, lysine methylation exhibits the most dynamic changes in the PN stage . To analyze the physiological functions of histone methylations, it is therefore important to elucidate the mechanism of epigenetic reprogramming. However, loss-of-function approaches using mutant histones whose lysine residues have been substituted with arginine residues are unable to erase histone modifications at all levels, since they are incapable of entirely replacing endogenous histones. To solve this problem, we used an alternative histone mutant whose lysine residues were substituted with methionine (K-M mutants). This mutant cannot be methylated itself but also prevents methylation of endogenous histones. We also developed a simple method for analyzing global transcription levels in early preimplantation embryos, involving using a commercial kit to examine the involvement of histone methylation in zygotic gene activation.
[Mh] Termos MeSH primário: Substituição de Aminoácidos
Histonas/metabolismo
Lisina/genética
Zigoto/metabolismo
[Mh] Termos MeSH secundário: Animais
Epigênese Genética
Regulação da Expressão Gênica no Desenvolvimento
Código das Histonas
Histonas/genética
Metionina/genética
Metilação
Camundongos
Mutação
Ativação Transcricional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); AE28F7PNPL (Methionine); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6988-3_18


  9 / 27657 MEDLINE  
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[PMID]:29326266
[Au] Autor:Pace L; Goudot C; Zueva E; Gueguen P; Burgdorf N; Waterfall JJ; Quivy JP; Almouzni G; Amigorena S
[Ad] Endereço:Institut Curie, PSL Research University, F-75005 Paris, France. luigia.pace@iigm.it genevieve.almouzni@curie.fr sebastian.amigorena@curie.fr.
[Ti] Título:The epigenetic control of stemness in CD8 T cell fate commitment.
[So] Source:Science;359(6372):177-186, 2018 Jan 12.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:After priming, naïve CD8 T lymphocytes establish specific heritable transcription programs that define progression to long-lasting memory cells or to short-lived effector cells. Although lineage specification is critical for protection, it remains unclear how chromatin dynamics contributes to the control of gene expression programs. We explored the role of gene silencing by the histone methyltransferase Suv39h1. In murine CD8 T cells activated after infection, Suv39h1-dependent trimethylation of histone H3 lysine 9 controls the expression of a set of stem cell-related memory genes. Single-cell RNA sequencing revealed a defect in silencing of stem/memory genes selectively in -defective T cell effectors. As a result, -defective CD8 T cells show sustained survival and increased long-term memory reprogramming capacity. Thus, Suv39h1 plays a critical role in marking chromatin to silence stem/memory genes during CD8 T effector terminal differentiation.
[Mh] Termos MeSH primário: Linfócitos T CD8-Positivos/imunologia
Linfócitos T CD8-Positivos/metabolismo
Inativação Gênica
Histona-Lisina N-Metiltransferase/metabolismo
Memória Imunológica
Listeriose/imunologia
Metiltransferases/metabolismo
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Células Cultivadas
Cromatina/metabolismo
Epigênese Genética
Feminino
Histona-Lisina N-Metiltransferase/genética
Histonas/metabolismo
Listeria monocytogenes/imunologia
Masculino
Metilação
Metiltransferases/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas Repressoras/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 0 (RNA, Messenger); 0 (Repressor Proteins); EC 2.1.1. (Suv39h1 protein, mouse); EC 2.1.1.- (Methyltransferases); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1126/science.aah6499


  10 / 27657 MEDLINE  
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[PMID]:29269482
[Au] Autor:Franks TM; McCloskey A; Shokirev MN; Benner C; Rathore A; Hetzer MW
[Ad] Endereço:Laboratory of Molecular and Cellular Biology, Salk Institute for Biological Studies, La Jolla, California 92037, USA.
[Ti] Título:Nup98 recruits the Wdr82-Set1A/COMPASS complex to promoters to regulate H3K4 trimethylation in hematopoietic progenitor cells.
[So] Source:Genes Dev;31(22):2222-2234, 2017 11 15.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies have shown that a subset of nucleoporins (Nups) can detach from the nuclear pore complex and move into the nuclear interior to regulate transcription. One such dynamic Nup, called Nup98, has been implicated in gene activation in healthy cells and has been shown to drive leukemogenesis when mutated in patients with acute myeloid leukemia (AML). Here we show that in hematopoietic cells, Nup98 binds predominantly to transcription start sites to recruit the Wdr82-Set1A/COMPASS (complex of proteins associated with Set1) complex, which is required for deposition of the histone 3 Lys4 trimethyl (H3K4me3)-activating mark. Depletion of Nup98 or Wdr82 abolishes Set1A recruitment to chromatin and subsequently ablates H3K4me3 at adjacent promoters. Furthermore, expression of a Nup98 fusion protein implicated in aggressive AML causes mislocalization of H3K4me3 at abnormal regions and up-regulation of associated genes. Our findings establish a function of Nup98 in hematopoietic gene activation and provide mechanistic insight into which Nup98 leukemic fusion proteins promote AML.
[Mh] Termos MeSH primário: Células-Tronco Hematopoéticas/metabolismo
Histona-Lisina N-Metiltransferase/metabolismo
Histonas/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Regiões Promotoras Genéticas
Ativação Transcricional
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Cromatina/metabolismo
Proteínas Cromossômicas não Histona/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Seres Humanos
Metilação
Camundongos
[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 (Histones); 0 (Nuclear Pore Complex Proteins); 0 (Wdr82 protein, mouse); 0 (nuclear pore complex protein 98); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.1101/gad.306753.117



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