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  1 / 4416 MEDLINE  
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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


  2 / 4416 MEDLINE  
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[PMID]:29236775
[Au] Autor:Wang F; Wang L; Wu J; Sokirniy I; Nguyen P; Bregnard T; Weinstock J; Mattern M; Bezsonova I; Hancock WW; Kumar S
[Ad] Endereço:Progenra Inc, Malvern, Pennsylvania, United States of America.
[Ti] Título:Active site-targeted covalent irreversible inhibitors of USP7 impair the functions of Foxp3+ T-regulatory cells by promoting ubiquitination of Tip60.
[So] Source:PLoS One;12(12):e0189744, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Accumulation of Foxp3+ T-regulatory (Treg) cells in the tumor microenvironment is associated with tumor immune evasion and poor patient outcome in the case of many solid tumors. Current therapeutic strategies for blocking Treg functions are not Treg-specific, and display only modest and transient efficacy. Recent studies revealed that ubiquitin-specific protease 7 (USP7) is essential for Treg functions by stabilizing expression of Tip60 and Foxp3, which together are central to the development and maintenance of the Treg cell lineage. Pharmacological inhibition of USP7 is therefore a promising strategy for suppressing Treg functions and promoting anti-tumor immunity. Previously, we reported the P5091 series of small molecule USP7 inhibitors and demonstrated their direct anti-tumor activity in vivo using xenograft models. However, the precise mechanism of action of these compounds was not well defined. In this study, we report the development and characterization of P217564, a second-generation USP7 inhibitor with improved potency and selectivity. P217564 selectively targets the catalytic cleft of USP7 and modifies its active site cysteine (C223) by forming a covalent adduct. Irreversible inhibition of USP7 results in durable downstream biological responses in cells, including down-regulation of Tip60 and consequent impairment of Treg suppressive function. In addition, we demonstrate that both USP7 and various USP7 substrates are subjected to Lys48-mediated ubiquitin modification, consistent with increased proteasomal degradation of these proteins because of USP7 inhibition.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Fatores de Transcrição Forkhead/metabolismo
Histona Acetiltransferases/metabolismo
Linfócitos T Reguladores/imunologia
Peptidase 7 Específica de Ubiquitina/antagonistas & inibidores
[Mh] Termos MeSH secundário: Domínio Catalítico
Linhagem Celular Tumoral
Seres Humanos
Inibidores de Proteases/farmacologia
Peptidase 7 Específica de Ubiquitina/metabolismo
Ubiquitinação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (FOXP3 protein, human); 0 (Forkhead Transcription Factors); 0 (Protease Inhibitors); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Tip60 protein, Drosophila); EC 3.4.19.12 (USP7 protein, human); EC 3.4.19.12 (Ubiquitin-Specific Peptidase 7)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189744


  3 / 4416 MEDLINE  
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[PMID]:29232376
[Au] Autor:Caliskan G; Baris IC; Ayaydin F; Dobson MJ; Senarisoy M; Boros IM; Topcu Z; Zencir S
[Ad] Endereço:Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Ege University, Izmir, Turkey.
[Ti] Título:Che1/AATF interacts with subunits of the histone acetyltransferase core module of SAGA complexes.
[So] Source:PLoS One;12(12):e0189193, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:General Control Non-derepressible 5 (GCN5) and Alteration/Deficiency in Activation 2 and 3 proteins (ADA2 and ADA3, respectively) are subunits of the Histone AcetylTransferase (HAT) module of SAGA- and ATAC-type co-activators. We previously reported four new interacting partners of human ADA3 identified by screening a human fetal brain cDNA library using yeast two hybrid technology. One of these partners was Apoptosis-Antagonizing Transcription Factor (AATF), also known as Che-1, an RNA polymerase II-binding protein with a number of roles in different cellular processes including regulation of transcription, cell proliferation, cell cycle control, DNA damage responses and apoptosis. Che-1/AATF is a potential therapeutic target for cancer treatments. In this study, we aimed to identify whether besides ADA3, other components of the HAT modules of SAGA and ATAC complexes, human ADA2 and GCN5 also interact with Che-1/AATF. Co-immunoprecipitation and co-localization experiments were used to demonstrate association of AATF both with two ADA2 isoforms, ADA2A and ADA2B and with GCN5 proteins in human cells and yeast two-hybrid assays to delineate domains in the ADA2 and GCN5 proteins required for these interactions. These findings provide new insights into the pathways regulated by ADA-containing protein complexes.
[Mh] Termos MeSH primário: Histona Acetiltransferases/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/metabolismo
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Seres Humanos
Ligação Proteica
Fatores de Transcrição/metabolismo
Ativação Transcricional
Fatores de Transcrição de p300-CBP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (SAGA complex, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (TADA2A protein, human); 0 (TADA2B protein, human); 0 (Trans-Activators); 0 (Transcription Factors); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.- (Sgf29 protein, human); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189193


  4 / 4416 MEDLINE  
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[PMID]:28450392
[Au] Autor:Wu D; Zhao L; Feng Z; Yu C; Ding J; Wang L; Wang F; Liu D; Zhu H; Xing F; Conaway JW; Conaway RC; Cai Y; Jin J
[Ad] Endereço:From the School of Life Sciences.
[Ti] Título:-Linked -acetylglucosamine transferase 1 regulates global histone H4 acetylation via stabilization of the nonspecific lethal protein NSL3.
[So] Source:J Biol Chem;292(24):10014-10025, 2017 06 16.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The human males absent on the first (MOF)-containing histone acetyltransferase nonspecific lethal (NSL) complex comprises nine subunits including the -linked -acetylglucosamine ( -GlcNAc) transferase, isoform 1 (OGT1). However, whether the -GlcNAc transferase activity of OGT1 controls histone acetyltransferase activity of the NSL complex and whether OGT1 physically interacts with the other NSL complex subunits remain unclear. Here, we demonstrate that OGT1 regulates the activity of the NSL complex by mainly acetylating histone H4 Lys-16, Lys-5, and Lys-8 via -GlcNAcylation and stabilization of the NSL complex subunit NSL3. Knocking down or overexpressing OGT1 in human cells remarkably affected the global acetylation of histone H4 residues Lys-16, Lys-5, and Lys-8. Because OGT1 is a subunit of the NSL complex, we also investigated the function of OGT1 in this complex. Co-transfection/co-immunoprecipitation experiments combined with -GlcNAc transferase assays confirmed that OGT1 specifically binds to and -GlcNAcylates NSL3. In addition, wheat germ agglutinin affinity purification verified the occurrence of -GlcNAc modification on NSL3 in cells. Moreover, -GlcNAcylation of NSL3 by wild-type OGT1 (OGT1-WT) stabilized NSL3. This stabilization was lost after co-transfection of NSL3 with an OGT1 mutant, OGT1 , that lacks -GlcNAc transferase activity. Furthermore, stabilization of NSL3 by OGT1-WT significantly increased the global acetylation levels of H4 Lys-5, Lys-8, and Lys-16 in cells. These results suggest that OGT1 regulates the activity of the NSL complex by stabilizing NSL3.
[Mh] Termos MeSH primário: Histona Acetiltransferases/metabolismo
Histonas/metabolismo
N-Acetilglucosaminiltransferases/metabolismo
Proteínas Nucleares/metabolismo
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Acetilação
Substituição de Aminoácidos
Animais
Células HEK293
Células HeLa
Histona Acetiltransferases/antagonistas & inibidores
Histona Acetiltransferases/química
Histona Acetiltransferases/genética
Seres Humanos
Isoenzimas/química
Isoenzimas/genética
Isoenzimas/metabolismo
N-Acetilglucosaminiltransferases/antagonistas & inibidores
N-Acetilglucosaminiltransferases/química
N-Acetilglucosaminiltransferases/genética
Proteínas Nucleares/antagonistas & inibidores
Proteínas Nucleares/química
Proteínas Nucleares/genética
Mutação Puntual
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Estabilidade Proteica
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Interferência de RNA
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Células Sf9
Spodoptera
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histones); 0 (Isoenzymes); 0 (KANSL3 protein, human); 0 (Nuclear Proteins); 0 (Protein Isoforms); 0 (Protein Subunits); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.4.1.- (N-Acetylglucosaminyltransferases); EC 2.4.1.- (UDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.781401


  5 / 4416 MEDLINE  
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[PMID]:29069084
[Au] Autor:Dahal BK; Kadyrova LY; Delfino KR; Rogozin IB; Gujar V; Lobachev KS; Kadyrov FA
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL, United States of America.
[Ti] Título:Involvement of DNA mismatch repair in the maintenance of heterochromatic DNA stability in Saccharomyces cerevisiae.
[So] Source:PLoS Genet;13(10):e1007074, 2017 Oct.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heterochromatin contains a significant part of nuclear DNA. Little is known about the mechanisms that govern heterochromatic DNA stability. We show here that in the yeast Saccharomyces cerevisiae (i) DNA mismatch repair (MMR) is required for the maintenance of heterochromatic DNA stability, (ii) MutLα (Mlh1-Pms1 heterodimer), MutSα (Msh2-Msh6 heterodimer), MutSß (Msh2-Msh3 heterodimer), and Exo1 are involved in MMR at heterochromatin, (iii) Exo1-independent MMR at heterochromatin frequently leads to the formation of Pol ζ-dependent mutations, (iv) MMR cooperates with the proofreading activity of Pol ε and the histone acetyltransferase Rtt109 in the maintenance of heterochromatic DNA stability, (v) repair of base-base mismatches at heterochromatin is less efficient than repair of base-base mismatches at euchromatin, and (vi) the efficiency of repair of 1-nt insertion/deletion loops at heterochromatin is similar to the efficiency of repair of 1-nt insertion/deletion loops at euchromatin.
[Mh] Termos MeSH primário: Reparo de Erro de Pareamento de DNA
DNA Fúngico/química
Heterocromatina
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Dano ao DNA
DNA Fúngico/genética
Exodesoxirribonucleases/genética
Genes pol
Histona Acetiltransferases/genética
Proteínas MutL/genética
Proteína MutS de Ligação de DNA com Erro de Pareamento/genética
Homologia de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Heterochromatin); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Rtt109 protein, S cerevisiae); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.11.1 (exodeoxyribonuclease I); EC 3.6.1.3 (MutL Proteins); EC 3.6.1.3 (MutS DNA Mismatch-Binding Protein)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171026
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007074


  6 / 4416 MEDLINE  
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[PMID]:29045464
[Au] Autor:Rajagopalan D; Pandey AK; Xiuzhen MC; Lee KK; Hora S; Zhang Y; Chua BH; Kwok HS; Bhatia SS; Deng LW; Tenen DG; Kappei D; Jha S
[Ad] Endereço:Cancer Science Institute of Singapore, National University of Singapore, Singapore.
[Ti] Título:TIP60 represses telomerase expression by inhibiting Sp1 binding to the TERT promoter.
[So] Source:PLoS Pathog;13(10):e1006681, 2017 Oct.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:HIV1-TAT interactive protein (TIP60) is a haploinsufficient tumor suppressor. However, the potential mechanisms endowing its tumor suppressor ability remain incompletely understood. It plays a vital role in virus-induced cancers where TIP60 down-regulates the expression of human papillomavirus (HPV) oncoprotein E6 which in turn destabilizes TIP60. This intrigued us to identify the role of TIP60, in the context of a viral infection, where it is targeted by oncoproteins. Through an array of molecular biology techniques such as Chromatin immunoprecipitation, expression analysis and mass spectrometry, we establish the hitherto unknown role of TIP60 in repressing the expression of the catalytic subunit of the human telomerase complex, TERT, a key driver for immortalization. TIP60 acetylates Sp1 at K639, thus inhibiting Sp1 binding to the TERT promoter. We identified that TIP60-mediated growth suppression of HPV-induced cervical cancer is mediated in part due to TERT repression through Sp1 acetylation. In summary, our study has identified a novel substrate for TIP60 catalytic activity and a unique repressive mechanism acting at the TERT promoter in virus-induced malignancies.
[Mh] Termos MeSH primário: Regulação Enzimológica da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Histona Acetiltransferases/metabolismo
Proteínas de Neoplasias/metabolismo
Elementos de Resposta
Fator de Transcrição Sp1/metabolismo
Telomerase/biossíntese
Neoplasias do Colo do Útero/metabolismo
[Mh] Termos MeSH secundário: Feminino
Células HeLa
Histona Acetiltransferases/genética
Seres Humanos
Lisina Acetiltransferase 5
Proteínas de Neoplasias/genética
Fator de Transcrição Sp1/genética
Telomerase/genética
Neoplasias do Colo do Útero/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neoplasm Proteins); 0 (Sp1 Transcription Factor); 0 (Sp1 protein, human); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (KAT5 protein, human); EC 2.3.1.48 (Lysine Acetyltransferase 5); EC 2.7.7.49 (TERT protein, human); EC 2.7.7.49 (Telomerase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006681


  7 / 4416 MEDLINE  
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[PMID]:28973436
[Au] Autor:Sun L; Luk E
[Ad] Endereço:Department of Biochemistry and Cell Biology, Stony Brook University, NY 11794-5215, USA.
[Ti] Título:Dual function of Swc5 in SWR remodeling ATPase activation and histone H2A eviction.
[So] Source:Nucleic Acids Res;45(17):9931-9946, 2017 Sep 29.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The chromatin remodeler SWR deposits histone H2A.Z at promoters and other regulatory sites via an ATP-driven histone exchange reaction that replaces nucleosomal H2A with H2A.Z. Simultaneous binding of SWR to both H2A nucleosome and free H2A.Z induces SWR ATPase activity and engages the histone exchange mechanism. Swc5 is a conserved subunit of the 14-polypeptide SWR complex that is required for the histone exchange reaction, but its molecular role is unknown. We found that Swc5, although not required for substrate binding, is required for SWR ATPase stimulation, suggesting that Swc5 is required to couple substrate recognition to ATPase activation. A biochemical complementation assay was developed to show that a unique, conserved domain at the C-terminus of Swc5, called Bucentaur (BCNT), is essential for the histone exchange activity of SWR, whereas an acidic region at the N-terminus is required for optimal SWR function. In vitro studies showed the acidic N-terminus of Swc5 preferentially binds to the H2A-H2B dimer and exhibits histone chaperone activity. We propose that an auxiliary function of Swc5 in SWR is to assist H2A ejection as H2A.Z is inserted into the nucleosome.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/química
Regulação Fúngica da Expressão Gênica
Histona Acetiltransferases/química
Histonas/química
Proteínas de Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/genética
Adenosina Trifosfatases/metabolismo
Montagem e Desmontagem da Cromatina
Teste de Complementação Genética
Histona Acetiltransferases/genética
Histona Acetiltransferases/metabolismo
Histonas/genética
Histonas/metabolismo
Nucleossomos/genética
Nucleossomos/metabolismo
Domínios Proteicos
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Transporte Proteico
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); 0 (Nucleosomes); 0 (Protein Isoforms); 0 (Saccharomyces cerevisiae Proteins); EC 2.3.1.48 (Histone Acetyltransferases); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx589


  8 / 4416 MEDLINE  
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[PMID]:28918903
[Au] Autor:Baptista T; Grünberg S; Minoungou N; Koster MJE; Timmers HTM; Hahn S; Devys D; Tora L
[Ad] Endereço:Institut de Génétique et de Biologie Moléculaire et Cellulaire, 67404 Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, 67404 Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, 67404 Illkirch, France; Université de Strasbourg, 67404 Illkirch, Fr
[Ti] Título:SAGA Is a General Cofactor for RNA Polymerase II Transcription.
[So] Source:Mol Cell;68(1):130-143.e5, 2017 Oct 05.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prior studies suggested that SAGA and TFIID are alternative factors that promote RNA polymerase II transcription, with about 10% of genes in S. cerevisiae dependent on SAGA. We reassessed the role of SAGA by mapping its genome-wide location and role in global transcription in budding yeast. We find that SAGA maps to the UAS elements of most genes, overlapping with Mediator binding and irrespective of previous designations of SAGA- or TFIID-dominated genes. Disruption of SAGA through mutation or rapid subunit depletion reduces transcription from nearly all genes, measured by newly synthesized RNA. We also find that the acetyltransferase Gcn5 synergizes with Spt3 to promote global transcription and that Spt3 functions to stimulate TBP recruitment at all tested genes. Our data demonstrate that SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription and is not consistent with the previous classification of SAGA- and TFIID-dominated genes.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica
Histona Acetiltransferases/genética
RNA Polimerase II/genética
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
Proteína de Ligação a TATA-Box/genética
Transativadores/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Deleção de Genes
Histona Acetiltransferases/metabolismo
Regiões Promotoras Genéticas
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
RNA Polimerase II/metabolismo
RNA Fúngico/genética
RNA Fúngico/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Fatores Associados à Proteína de Ligação a TATA/genética
Fatores Associados à Proteína de Ligação a TATA/metabolismo
Proteína de Ligação a TATA-Box/metabolismo
Transativadores/metabolismo
Fatores de Transcrição/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 0 (RNA, Fungal); 0 (SAGA complex, S cerevisiae); 0 (SPT15 protein, S cerevisiae); 0 (SPT3 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (TATA-Binding Protein Associated Factors); 0 (TATA-Box Binding Protein); 0 (Trans-Activators); 0 (Transcription Factors); EC 2.3.1.48 (GCN5 protein, S cerevisiae); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE


  9 / 4416 MEDLINE  
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[PMID]:28892470
[Au] Autor:Kwon HK; Chen HM; Mathis D; Benoist C
[Ad] Endereço:Division of Immunology, Department of Microbiology and Immunobiology, Harvard Medical School, and Evergrande Center for Immunologic Diseases, Harvard Medical School and Brigham and Women's Hospital, Boston, Massachusetts, USA.
[Ti] Título:Different molecular complexes that mediate transcriptional induction and repression by FoxP3.
[So] Source:Nat Immunol;18(11):1238-1248, 2017 Nov.
[Is] ISSN:1529-2916
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:FoxP3 conditions the transcriptional signature and functional facets of regulatory T cells (T cells). Its mechanism of action, whether as an activator or a repressor, has remained unclear. Here, chromatin analysis showed that FoxP3 bound active enhancer elements, not repressed chromatin, around loci over- or under-expressed in T cells. We evaluated the impact of a panel of FoxP3 mutants on its transcriptional activity and interactions with DNA, transcriptional cofactors and chromatin. Computational integration, confirmed by biochemical interaction and size analyses, showed that FoxP3 existed in distinct multimolecular complexes. It was active and primarily an activator when complexed with the transcriptional factors RELA, IKZF2 and KAT5. In contrast, FoxP3 was inactive when complexed with the histone methyltransferase EZH2 and transcription factors YY1 and IKZF3. The latter complex partitioned to a peripheral region of the nucleus, as shown by super-resolution microscopy. Thus, FoxP3 acts in multimodal fashion to directly activate or repress transcription, in a context- and partner-dependent manner, to govern T cell phenotypes.
[Mh] Termos MeSH primário: Fatores de Transcrição Forkhead/genética
Regulação da Expressão Gênica
Linfócitos T Reguladores/metabolismo
Ativação Transcricional
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
DNA/genética
DNA/metabolismo
Fatores de Transcrição Forkhead/imunologia
Fatores de Transcrição Forkhead/metabolismo
Perfilação da Expressão Gênica/métodos
Histona Acetiltransferases/genética
Histona Acetiltransferases/metabolismo
Histona-Lisina N-Metiltransferase/genética
Histona-Lisina N-Metiltransferase/metabolismo
Immunoblotting
Lisina Acetiltransferase 5
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Mutação
Células NIH 3T3
Ligação Proteica
Linfócitos T Reguladores/imunologia
Transativadores/genética
Transativadores/metabolismo
Fator de Transcrição RelA/genética
Fator de Transcrição RelA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Forkhead Transcription Factors); 0 (Foxp3 protein, mouse); 0 (Rela protein, mouse); 0 (Trans-Activators); 0 (Transcription Factor RelA); 9007-49-2 (DNA); EC 2.1.1.- (histone methyltransferase); EC 2.1.1.43 (Histone-Lysine N-Methyltransferase); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Kat5 protein, mouse); EC 2.3.1.48 (Lysine Acetyltransferase 5)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE
[do] DOI:10.1038/ni.3835


  10 / 4416 MEDLINE  
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[PMID]:28887412
[Au] Autor:Li X; Seidel CW; Szerszen LT; Lange JJ; Workman JL; Abmayr SM
[Ad] Endereço:Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.
[Ti] Título:Enzymatic modules of the SAGA chromatin-modifying complex play distinct roles in gene expression and development.
[So] Source:Genes Dev;31(15):1588-1600, 2017 Aug 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Spt-Ada-Gcn5-acetyltransferase (SAGA) chromatin-modifying complex is a transcriptional coactivator that contains four different modules of subunits. The intact SAGA complex has been well characterized for its function in transcription regulation and development. However, little is known about the roles of individual modules within SAGA and whether they have any SAGA-independent functions. Here we demonstrate that the two enzymatic modules of SAGA are differently required in oogenesis. Loss of the histone acetyltransferase (HAT) activity blocks oogenesis, while loss of the H2B deubiquitinase (DUB) activity does not. However, the DUB module regulates a subset of genes in early embryogenesis, and loss of the DUB subunits causes defects in embryogenesis. ChIP-seq (chromatin immunoprecipitation [ChIP] combined with high-throughput sequencing) analysis revealed that both the DUB and HAT modules bind most SAGA target genes even though many of these targets do not require the DUB module for expression. Furthermore, we found that the DUB module can bind to chromatin and regulate transcription independently of the HAT module. Our results suggest that the DUB module has functions within SAGA and independent functions.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/crescimento & desenvolvimento
Drosophila melanogaster/genética
Regulação da Expressão Gênica no Desenvolvimento
Histona Acetiltransferases/metabolismo
Oogênese/genética
[Mh] Termos MeSH secundário: Animais
Ataxina-7/genética
Cromatina/metabolismo
Enzimas Desubiquitinantes/metabolismo
Proteínas de Drosophila/genética
Feminino
Sequenciamento de Nucleotídeos em Larga Escala
Histona Acetiltransferases/genética
Histonas/metabolismo
Microscopia Confocal
Ovário/crescimento & desenvolvimento
Ligação Proteica
Zigoto/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ataxin-7); 0 (Chromatin); 0 (Drosophila Proteins); 0 (Histones); EC 2.3.1.48 (ADA2 protein, Drosophila); EC 2.3.1.48 (Histone Acetyltransferases); EC 2.3.1.48 (Pcaf protein, Drosophila); EC 3.4.19.12 (Deubiquitinating Enzymes)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170910
[St] Status:MEDLINE
[do] DOI:10.1101/gad.300988.117



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