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Pesquisa : D08.811.277.087.520.750 [Categoria DeCS]
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[PMID]:28468907
[Au] Autor:Demin AA; Lee M; Lee CH; Seo YS
[Ad] Endereço:Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Daejeon 34141, Korea and.
[Ti] Título:GSK-3ß Homolog Rim11 and the Histone Deacetylase Complex Ume6-Sin3-Rpd3 Are Involved in Replication Stress Response Caused by Defects in Dna2.
[So] Source:Genetics;206(2):829-842, 2017 06.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lagging strand synthesis is mechanistically far more complicated than leading strand synthesis because it involves multistep processes and requires considerably more enzymes and protein factors. Due to this complexity, multiple fail-safe factors are required to ensure successful replication of the lagging strand DNA. We attempted to identify novel factors that are required in the absence of the helicase activity of Dna2, an essential enzyme in Okazaki-fragment maturation. In this article, we identified Rim11, a GSK-3ß-kinase homolog, as a multicopy suppressor of helicase-dead mutant ( ). Subsequent epistasis analysis revealed that Ume6 (a DNA binding protein, a downstream substrate of Rim11) also acted as a multicopy suppressor of the allele. We found that the interaction of Ume6 with the conserved histone deacetylase complex Sin3-Rpd3 and the catalytic activity of Rpd3 were indispensable for the observed suppression of the mutant. Moreover, multicopy suppression by Rim11/Ume6 requires the presence of sister-chromatid recombination mediated by Rad52/Rad59 proteins, but not vice versa. Interestingly, the overexpression of Rim11 or Ume6 also suppressed the MMS sensitivity of Δ. We also showed that the lethality of helicase-dead mutant was attributed to checkpoint activation and that decreased levels of deoxynucleotide triphosphates (dNTPs) by overexpressing Sml1 (an inhibitor of ribonucleotide reductase) rescued the mutant. We also present evidence that indicates Rim11/Ume6 works independently but in parallel with that of checkpoint inhibition, dNTP regulation, and sister-chromatid recombination. In conclusion, our results establish Rim11, Ume6, the histone deacetylase complex Sin3-Rpd3 and Sml1 as new factors important in the events of faulty lagging strand synthesis.
[Mh] Termos MeSH primário: DNA Helicases/genética
Histona Desacetilases/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
Proteínas Serina-Treonina Quinases/genética
Proteínas Repressoras/genética
Proteínas de Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: DNA/genética
Replicação do DNA/genética
Glicogênio Sintase Quinase 3 beta/genética
Proteínas Mutantes/genética
Saccharomyces cerevisiae/genética
Complexo Correpressor Histona Desacetilase e Sin3/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); 0 (Mutant Proteins); 0 (Okazaki fragments); 0 (Repressor Proteins); 0 (SIN3 protein, S cerevisiae); 0 (SML1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (UME6 protein, S cerevisiae); 9007-49-2 (DNA); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (RIM11 protein, S cerevisiae); EC 3.5.1.- (RPD3 protein, S cerevisiae); EC 3.5.1.98 (Histone Deacetylases); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (DNA2 protein, S cerevisiae)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171213
[Lr] Data última revisão:
171213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.116.198671


  2 / 78 MEDLINE  
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[PMID]:26522936
[Au] Autor:Clark MD; Zhang Y; Radhakrishnan I
[Ad] Endereço:Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
[Ti] Título:Solution NMR Studies of an Alternative Mode of Sin3 Engagement by the Sds3 Subunit in the Histone Deacetylase-Associated Sin3L/Rpd3L Corepressor Complex.
[So] Source:J Mol Biol;427(24):3817-23, 2015 Dec 04.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The Sds3 transcriptional corepressor facilitates the assembly of the 1- to 2-MDa histone deacetylase-associated Sin3L/Rpd3L complex by providing a crucial homodimerization activity. Sds3 engages the scaffolding protein Sin3A, via a bipartite motif within the Sin3 interaction domain (SID) comprising a helix and an extended segment. Here, we show that the SID samples two discrete, substantially populated conformations with lifetimes in the tens of milliseconds range. The two conformations differ via a translation of the main chain and the corresponding side chains in the 5- to 7-Å range. Given the close proximity of the SID to other functional motifs in Sds3 at the sequence level, the conformational exchange has the potential to regulate these activities.
[Mh] Termos MeSH primário: Histona Desacetilase 1/química
Proteínas Repressoras/química
Complexo Correpressor Histona Desacetilase e Sin3/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Seres Humanos
Modelos Moleculares
Dados de Sequência Molecular
Ressonância Magnética Nuclear Biomolecular
Ligação Proteica
Subunidades Proteicas
Soluções
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Subunits); 0 (Repressor Proteins); 0 (SDS3 protein, human); 0 (Solutions); EC 3.5.1.98 (HDAC1 protein, human); EC 3.5.1.98 (Histone Deacetylase 1); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151103
[St] Status:MEDLINE


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[PMID]:25133314
[Au] Autor:Barnes VL; Bhat A; Unnikrishnan A; Heydari AR; Arking R; Pile LA
[Ad] Endereço:Department of Biological Sciences, Wayne State University, Detroit, Michigan, 48202, USA.
[Ti] Título:SIN3 is critical for stress resistance and modulates adult lifespan.
[So] Source:Aging (Albany NY);6(8):645-60, 2014 Aug.
[Is] ISSN:1945-4589
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Coordinate control of gene activity is critical for fitness and longevity of an organism. The SIN3 histone deacetylase (HDAC) complex functions as a transcriptional repressor of many genes. SIN3-regulated genes include those that encode proteins affecting multiple aspects of mitochondrial function, such as energy production and stress responsiveness, important for health maintenance. Here we used Drosophila melanogaster as a model organism to examine the role of SIN3 in the regulation of fitness and longevity. Adult flies with RNA interference (RNAi) induced knockdown expression of Sin3A have reduced climbing ability; an activity that likely requires fully functional mitochondria. Additionally, compared to wild type, adult Sin3A knockdown flies were more sensitive to oxidative stress. Interestingly, media supplementation with the antioxidant glutathione largely restored fly tolerance to oxidative stress. Although Sin3A knockdown flies exhibited decreased longevity compared to wild type, no significant changes in expression of many well-categorized aging genes were observed. We found, however, that Sin3A knockdown corresponded to a significant reduction in expression of genes encoding proteins involved in the de novo synthesis of glutathione. Taken together, the data support a model whereby SIN3 regulates a gene expression program required for proper mitochondrial function and effective stress response during adulthood.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Longevidade/fisiologia
Estresse Oxidativo/fisiologia
Complexo Correpressor Histona Desacetilase e Sin3/metabolismo
Estresse Fisiológico/fisiologia
[Mh] Termos MeSH secundário: Animais
Comportamento Animal/fisiologia
Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Drosophila melanogaster/metabolismo
Atividade Motora/fisiologia
Interferência de RNA
Complexo Correpressor Histona Desacetilase e Sin3/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140819
[St] Status:MEDLINE


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[PMID]:25076120
[Au] Autor:Zheng Y; Tabbaa ZM; Khan Z; Schoolmeester JK; El-Nashar S; Famuyide A; Keeney GL; Daftary GS
[Ad] Endereço:Laboratory of Translational Epigenetics in Reproduction (Y.Z., Z.M.T., Z.K., G.S.D.) and Departments of Laboratory Medicine and Pathology (J.K.S., G.L.K.) and Obstetrics and Gynecology (Y.Z., Z.M.T., Z.K., S.E.-N., A.F., G.S.D.), Mayo Clinic, Rochester, Minnesota 55905.
[Ti] Título:Epigenetic regulation of uterine biology by transcription factor KLF11 via posttranslational histone deacetylation of cytochrome p450 metabolic enzymes.
[So] Source:Endocrinology;155(11):4507-20, 2014 Nov.
[Is] ISSN:1945-7170
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Endocrine regulation of uterine biology is critical for embryo receptivity and human reproduction. Uterine endometrium depends on extrinsic sex steroid input and hence likely has mechanisms that enable adaptation to hormonal variation. Emerging evidence suggests that sex steroid bioavailability in the endometrium is determined by adjusting their metabolic rate and fate via regulation of cytochrome (CYP) p450 enzymes. The CYP enzymes are targeted by ubiquitously expressed Sp/Krüppel-like (Sp/KLF) transcription factors. Specifically, KLF11 is highly expressed in reproductive tissues, regulates an array of endocrine/metabolic pathways via epigenetic histone-based mechanisms and, when aberrantly expressed, is associated with diabetes and reproductive tract diseases, such as leiomyoma and endometriosis. Using KLF11 as a model to investigate epigenetic regulation of endometrial first-pass metabolism, we evaluated the expression of a comprehensive array of metabolic enzymes in Ishikawa cells. KLF11 repressed most endometrial CYP enzymes. To characterize KLF11-recruited epigenetic regulatory mechanisms, we focused on the estrogen-metabolizing enzyme CYP3A4. KLF11 expression declined in secretory phase endometrial epithelium associated with increased CYP3A4 expression. Additionally, KLF11 bound to CYP3A4 promoter GC elements and thereby repressed promoter, message, protein as well as enzymatic function. This repression was epigenetically mediated, because KLF11 colocalized with and recruited the corepressor SIN3A/histone deacetylase resulting in selective deacetylation of the CYP3A4 promoter. Repression was reversed by a mutation in KLF11 that abrogated cofactor recruitment and binding. This repression was also pharmacologically reversible with an histone deacetylase inhibitor. Pharmacological alteration of endometrial metabolism could have long-term translational implications on human reproduction and uterine disease.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/fisiologia
Sistema Enzimático do Citocromo P-450/genética
Epigênese Genética/fisiologia
Histonas/metabolismo
Proteínas Repressoras/fisiologia
Complexo Correpressor Histona Desacetilase e Sin3/metabolismo
Útero/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Sistema Enzimático do Citocromo P-450/metabolismo
Feminino
Perfilação da Expressão Gênica
Seres Humanos
Análise em Microsséries
Processamento de Proteína Pós-Traducional/genética
Células Tumorais Cultivadas
Útero/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Histones); 0 (KLF11 protein, human); 0 (Repressor Proteins); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1412
[Cu] Atualização por classe:141018
[Lr] Data última revisão:
141018
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:140731
[St] Status:MEDLINE
[do] DOI:10.1210/en.2014-1139


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[PMID]:25073741
[Au] Autor:Sardiu ME; Smith KT; Groppe BD; Gilmore JM; Saraf A; Egidy R; Peak A; Seidel CW; Florens L; Workman JL; Washburn MP
[Ad] Endereço:From the ‡Stowers Institute for Medical Research, Kansas City, Missouri 64110;
[Ti] Título:Suberoylanilide hydroxamic acid (SAHA)-induced dynamics of a human histone deacetylase protein interaction network.
[So] Source:Mol Cell Proteomics;13(11):3114-25, 2014 Nov.
[Is] ISSN:1535-9484
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histone deacetylases (HDACs) are targets for cancer therapy. Suberoylanilide hydroxamic acid (SAHA) is an HDAC inhibitor approved by the U.S. Food and Drug Administration for the treatment of cutaneous T-cell lymphoma. To obtain a better mechanistic understanding of the Sin3/HDAC complex in cancer, we extended its protein-protein interaction network and identified a mutually exclusive pair within the complex. We then assessed the effects of SAHA on the disruption of the complex network through six homologous baits. SAHA perturbs multiple protein interactions and therefore compromises the composition of large parts of the Sin3/HDAC network. A comparison of the effect of SAHA treatment on gene expression in breast cancer cells to a knockdown of the ING2 subunit indicated that a portion of the anticancer effects of SAHA may be attributed to the disruption of ING2's association with the complex. Our dynamic protein interaction network resource provides novel insights into the molecular mechanism of SAHA action and demonstrates the potential for drugs to rewire networks.
[Mh] Termos MeSH primário: Inibidores de Histona Desacetilases/farmacologia
Histona Desacetilases/metabolismo
Proteínas de Homeodomínio/genética
Ácidos Hidroxâmicos/farmacologia
Mapas de Interação de Proteínas
Receptores Citoplasmáticos e Nucleares/genética
Complexo Correpressor Histona Desacetilase e Sin3/metabolismo
Proteínas Supressoras de Tumor/genética
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Feminino
Expressão Gênica/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Ligação Proteica
Neoplasias de Mama Triplo Negativas/tratamento farmacológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Histone Deacetylase Inhibitors); 0 (Homeodomain Proteins); 0 (Hydroxamic Acids); 0 (ING2 protein, human); 0 (Receptors, Cytoplasmic and Nuclear); 0 (Tumor Suppressor Proteins); 58IFB293JI (vorinostat); EC 3.5.1.98 (Histone Deacetylases); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140731
[St] Status:MEDLINE
[do] DOI:10.1074/mcp.M113.037127


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[PMID]:24944246
[Au] Autor:Xiong Y; Svingen PA; Sarmento OO; Smyrk TC; Dave M; Khanna S; Lomberk GA; Urrutia RA; Faubion WA
[Ad] Endereço:Epigenetics and Chromatin Dynamics Laboratory, Mayo Clinic, Rochester, Minnesota; Division of Gastroenterology and Hepatology, Mayo Clinic, Rochester, Minnesota;
[Ti] Título:Differential coupling of KLF10 to Sin3-HDAC and PCAF regulates the inducibility of the FOXP3 gene.
[So] Source:Am J Physiol Regul Integr Comp Physiol;307(6):R608-20, 2014 Sep 15.
[Is] ISSN:1522-1490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inducible gene expression, which requires chromatin remodeling on gene promoters, underlies the epigenetically inherited differentiation program of most immune cells. However, chromatin-mediated mechanisms that underlie these events in T regulatory cells remain to be fully characterized. Here, we report that inducibility of FOXP3, a key transcription factor for the development of T regulatory cells, depends upon Kruppel-like factor 10 (KLF10) interacting with two antagonistic histone-modifying systems. We utilized chromatin immunoprecipitation, genome-integrated reporter assays, and functional domain KLF10 mutant proteins, to characterize reciprocal interactions between this transcription factor and either the Sin3-histone deacetylase complex or the histone acetyltransferase, p300/CBP-associated factor (PCAF). We characterize a Sin3-interacting repressor domain on the NH2 terminus of KLF10, which works to limit the activating function of this transcription factor. Indeed, inactivation of this Sin3-interacting domain renders KLF10 able to physically associate with PCAF as to induce FOXP3 gene transcription. We show that this biochemical data derived from studying our genome-integrated reporter cell system are recapitulated in primary murine lymphocytes. Collectively, these results advance our understanding of how a single transcription factor, namely KLF10, functions as a toggle to integrate antagonistic signals regulating FOXP3 and, thus, immune activation.
[Mh] Termos MeSH primário: Colite/enzimologia
Colo/enzimologia
Fatores de Transcrição de Resposta de Crescimento Precoce/metabolismo
Fatores de Transcrição Forkhead/metabolismo
Fatores de Transcrição Kruppel-Like/metabolismo
Complexo Correpressor Histona Desacetilase e Sin3/metabolismo
Linfócitos T Reguladores/enzimologia
Fatores de Transcrição de p300-CBP/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Montagem e Desmontagem da Cromatina
Colite/induzido quimicamente
Colite/genética
Colite/imunologia
Colo/imunologia
Sulfato de Dextrana
Modelos Animais de Doenças
Fatores de Transcrição de Resposta de Crescimento Precoce/química
Fatores de Transcrição de Resposta de Crescimento Precoce/deficiência
Fatores de Transcrição de Resposta de Crescimento Precoce/genética
Epigênese Genética
Fatores de Transcrição Forkhead/genética
Seres Humanos
Células Jurkat
Fatores de Transcrição Kruppel-Like/química
Fatores de Transcrição Kruppel-Like/deficiência
Fatores de Transcrição Kruppel-Like/genética
Camundongos
Camundongos Knockout
Modelos Moleculares
Mutação
Regiões Promotoras Genéticas
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Transdução de Sinais
Complexo Correpressor Histona Desacetilase e Sin3/química
Linfócitos T Reguladores/imunologia
Transfecção
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Early Growth Response Transcription Factors); 0 (FOXP3 protein, human); 0 (Forkhead Transcription Factors); 0 (Foxp3 protein, mouse); 0 (KLF10 protein, human); 0 (KLF10 protein, mouse); 0 (Kruppel-Like Transcription Factors); 9042-14-2 (Dextran Sulfate); EC 2.3.1.48 (p300-CBP Transcription Factors); EC 2.3.1.48 (p300-CBP-associated factor); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140620
[St] Status:MEDLINE
[do] DOI:10.1152/ajpregu.00085.2014


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[PMID]:24838945
[Au] Autor:Aihara M; Jin X; Kurihara Y; Yoshida Y; Matsushima Y; Oku M; Hirota Y; Saigusa T; Aoki Y; Uchiumi T; Yamamoto T; Sakai Y; Kang D; Kanki T
[Ad] Endereço:Department of Clinical Chemistry and Laboratory Medicine, Kyushu University Graduate School of Medical Sciences, Fukuoka 812-8582, Japan.
[Ti] Título:Tor and the Sin3-Rpd3 complex regulate expression of the mitophagy receptor protein Atg32 in yeast.
[So] Source:J Cell Sci;127(Pt 14):3184-96, 2014 Jul 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:When mitophagy is induced in Saccharomyces cerevisiae, the mitochondrial outer membrane protein ScAtg32 interacts with the cytosolic adaptor protein ScAtg11. ScAtg11 then delivers the mitochondria to the pre-autophagosomal structure for autophagic degradation. Despite the importance of ScAtg32 for mitophagy, the expression and functional regulation of ScAtg32 are poorly understood. In this study, we identified and characterized the ScAtg32 homolog in Pichia pastoris (PpAtg32). Interestingly, we found that PpAtg32 was barely expressed before induction of mitophagy and was rapidly expressed after induction of mitophagy by starvation. Additionally, PpAtg32 was phosphorylated when mitophagy was induced. We found that PpAtg32 expression was suppressed by Tor and the downstream PpSin3-PpRpd3 complex. Inhibition of Tor by rapamycin induced PpAtg32 expression, but could neither phosphorylate PpAtg32 nor induce mitophagy. Based on these findings, we conclude that the Tor and PpSin3-PpRpd3 pathway regulates PpAtg32 expression, but not PpAtg32 phosphorylation.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Receptores Citoplasmáticos e Nucleares/genética
Receptores Citoplasmáticos e Nucleares/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
Complexo Correpressor Histona Desacetilase e Sin3/metabolismo
[Mh] Termos MeSH secundário: Proteínas Relacionadas à Autofagia
Ligação Proteica
Saccharomyces cerevisiae/citologia
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Atg32 protein, S cerevisiae); 0 (Autophagy-Related Proteins); 0 (Receptors, Cytoplasmic and Nuclear); 0 (Saccharomyces cerevisiae Proteins); 0 (Vesicular Transport Proteins); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140520
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.153254


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[PMID]:24282621
[Au] Autor:Adamson SW; Browning RE; Budachetri K; Ribeiro JM; Karim S
[Ad] Endereço:Department of Biological Sciences, the University of Southern Mississippi, Hattiesburg, Mississippi, United States of America.
[Ti] Título:Knockdown of selenocysteine-specific elongation factor in Amblyomma maculatum alters the pathogen burden of Rickettsia parkeri with epigenetic control by the Sin3 histone deacetylase corepressor complex.
[So] Source:PLoS One;8(11):e82012, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Selenocysteine is the 21st naturally-occurring amino acid. Selenoproteins have diverse functions and many remain uncharacterized, but they are typically associated with antioxidant activity. The incorporation of selenocysteine into the nascent polypeptide chain recodes the TGA stop codon and this process depends upon a number of essential factors including the selenocysteine elongation factor (SEF). The transcriptional expression of SEF did not change significantly in tick midguts throughout the blood meal, but decreased in salivary glands to 20% at the end of the fast feeding phase. Since selenoprotein translation requires this specialized elongation factor, we targeted this gene for knockdown by RNAi to gain a global view of the role selenoproteins play in tick physiology. We found no significant differences in tick engorgement and embryogenesis but detected no antioxidant capacity in tick saliva. The transcriptional profile of selenoproteins in R. parkeri-infected Amblyomma maculatum revealed declined activity of selenoprotein M and catalase and increased activity of selenoprotein O, selenoprotein S, and selenoprotein T. Furthermore, the pathogen burden was significantly altered in SEF-knockdowns. We then determined the global impact of SEF-knockdown by RNA-seq, and mapped huge shifts in secretory gene expression that could be the result of downregulation of the Sin3 histone deacetylase corepressor complex.
[Mh] Termos MeSH primário: Epigênese Genética
Técnicas de Silenciamento de Genes
Ixodidae/microbiologia
Fatores de Alongamento de Peptídeos/genética
Rickettsia/isolamento & purificação
Selenocisteína/metabolismo
Complexo Correpressor Histona Desacetilase e Sin3/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Regulação da Expressão Gênica
Dados de Sequência Molecular
Fatores de Alongamento de Peptídeos/química
Fatores de Alongamento de Peptídeos/metabolismo
Filogenia
Rickettsia/genética
Selenoproteínas/genética
Homologia de Sequência de Aminoácidos
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, N.I.H., INTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Peptide Elongation Factors); 0 (Selenoproteins); 0CH9049VIS (Selenocysteine); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1408
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0082012


  9 / 78 MEDLINE  
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[PMID]:24189169
[Au] Autor:Kadamb R; Mittal S; Bansal N; Batra H; Saluja D
[Ad] Endereço:Dr. B.R. Ambedkar Center for Biomedical Research, University of Delhi, Delhi 110007, India. Electronic address: ramakadamb@gmail.com.
[Ti] Título:Sin3: insight into its transcription regulatory functions.
[So] Source:Eur J Cell Biol;92(8-9):237-46, 2013 Aug-Sep.
[Is] ISSN:1618-1298
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Sin3, a large acidic protein, shares structural similarity with the helix-loop-helix dimerization domain of proteins of the Myc family of transcription factors. Sin3/HDAC corepressor complex functions in transcriptional regulation of several genes and is therefore implicated in the regulation of key biological processes. Knockdown studies have confirmed the role of Sin3 in cellular proliferation, differentiation, apoptosis and cell cycle regulation, emphasizing Sin3 as an essential regulator of critical cellular events in normal and pathological processes. The present review covers the diverse functions of this master transcriptional regulator as well as illustrates the redundant and distinct functions of its two mammalian isoforms.
[Mh] Termos MeSH primário: Proteínas Repressoras/genética
Complexo Correpressor Histona Desacetilase e Sin3/genética
[Mh] Termos MeSH secundário: Animais
Ciclo Celular
Transformação Celular Neoplásica/metabolismo
Proteínas de Drosophila/química
Proteínas de Drosophila/genética
Proteínas de Drosophila/metabolismo
Estabilidade Enzimática
Proteínas Fúngicas/química
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Regulação da Expressão Gênica
Histonas/genética
Histonas/metabolismo
Seres Humanos
Redes e Vias Metabólicas
Isoformas de Proteínas/química
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Proteínas Repressoras/química
Proteínas Repressoras/metabolismo
Complexo Correpressor Histona Desacetilase e Sin3/química
Complexo Correpressor Histona Desacetilase e Sin3/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Fungal Proteins); 0 (Histones); 0 (Protein Isoforms); 0 (Repressor Proteins); 0 (SIN3A transcription factor); 0 (SIN3B protein, human); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:131202
[Lr] Data última revisão:
131202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131106
[St] Status:MEDLINE


  10 / 78 MEDLINE  
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[PMID]:23612983
[Au] Autor:Khan DH; He S; Yu J; Winter S; Cao W; Seiser C; Davie JR
[Ad] Endereço:Manitoba Institute of Child Health, University of Manitoba, Winnipeg, Manitoba R3E 3P4, Canada.
[Ti] Título:Protein kinase CK2 regulates the dimerization of histone deacetylase 1 (HDAC1) and HDAC2 during mitosis.
[So] Source:J Biol Chem;288(23):16518-28, 2013 Jun 07.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Histone deacetylase 1 (HDAC1) and HDAC2 are components of corepressor complexes that are involved in chromatin remodeling and regulation of gene expression by regulating dynamic protein acetylation. HDAC1 and -2 form homo- and heterodimers, and their activity is dependent upon dimer formation. Phosphorylation of HDAC1 and/or HDAC2 in interphase cells is required for the formation of HDAC corepressor complexes. In this study, we show that during mitosis, HDAC2 and, to a lesser extent, HDAC1 phosphorylation levels dramatically increase. When HDAC1 and -2 are displaced from the chromosome during metaphase, they dissociate from each other, but each enzyme remains in association with components of the HDAC corepressor complexes Sin3, NuRD, and CoREST as homodimers. Enzyme inhibition studies and mutational analyses demonstrated that protein kinase CK2-catalyzed phosphorylation of HDAC1 and -2 is crucial for the dissociation of these two enzymes. These results suggest that corepressor complexes, including HDAC1 or HDAC2 homodimers, might target different cellular proteins during mitosis.
[Mh] Termos MeSH primário: Caseína Quinase I/metabolismo
Cromossomos Humanos/enzimologia
Histona Desacetilase 1/metabolismo
Histona Desacetilase 2/metabolismo
Mitose/fisiologia
Multimerização Proteica/fisiologia
[Mh] Termos MeSH secundário: Caseína Quinase I/antagonistas & inibidores
Caseína Quinase I/genética
Cromossomos Humanos/genética
Proteínas Correpressoras
Células HEK293
Células HeLa
Histona Desacetilase 1/genética
Histona Desacetilase 2/genética
Seres Humanos
Complexo Mi-2 de Remodelação de Nucleossomo e Desacetilase/genética
Complexo Mi-2 de Remodelação de Nucleossomo e Desacetilase/metabolismo
Mutação
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
Fosforilação/fisiologia
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Complexo Correpressor Histona Desacetilase e Sin3/genética
Complexo Correpressor Histona Desacetilase e Sin3/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Co-Repressor Proteins); 0 (Nerve Tissue Proteins); 0 (RCOR1 protein, human); 0 (Repressor Proteins); EC 2.7.11.1 (Casein Kinase I); EC 3.5.1.98 (HDAC1 protein, human); EC 3.5.1.98 (HDAC2 protein, human); EC 3.5.1.98 (Histone Deacetylase 1); EC 3.5.1.98 (Histone Deacetylase 2); EC 3.5.1.98 (Mi-2 Nucleosome Remodeling and Deacetylase Complex); EC 3.5.1.98 (Sin3 Histone Deacetylase and Corepressor Complex)
[Em] Mês de entrada:1308
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130425
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M112.440446



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