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Pesquisa : D12.776.260.775.186 [Categoria DeCS]
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[PMID]:28453628
[Au] Autor:Svetoni F; De Paola E; La Rosa P; Mercatelli N; Caporossi D; Sette C; Paronetto MP
[Ad] Endereço:Department of Movement, Human and Health Sciences, University of Rome "Foro Italico", 00135 Rome, Italy.
[Ti] Título:Post-transcriptional regulation of FUS and EWS protein expression by miR-141 during neural differentiation.
[So] Source:Hum Mol Genet;26(14):2732-2746, 2017 07 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Brain development involves proliferation, migration and specification of neural progenitor cells, culminating in neuronal circuit formation. Mounting evidence indicates that improper regulation of RNA binding proteins (RBPs), including members of the FET (FUS, EWS, TAF15) family, results in defective cortical development and/or neurodegenerative disorders. However, in spite of their physiological relevance, the precise pattern of FET protein expression in developing neurons is largely unknown. Herein, we found that FUS, EWS and TAF15 expression is differentially regulated during brain development, both in time and in space. In particular, our study identifies a fine-tuned regulation of FUS and EWS during neuronal differentiation, whereas TAF15 appears to be more constitutively expressed. Mechanistically FUS and EWS protein expression is regulated at the post-transcriptional level during neuron differentiation and brain development. Moreover, we identified miR-141 as a key regulator of these FET proteins that modulate their expression levels in differentiating neuronal cells. Thus, our studies uncover a novel link between post-transcriptional regulation of FET proteins expression and neurogenesis.
[Mh] Termos MeSH primário: MicroRNAs/metabolismo
Neurônios/fisiologia
Processamento Pós-Transcricional do RNA
Proteína EWS de Ligação a RNA/biossíntese
Proteína FUS de Ligação a RNA/biossíntese
[Mh] Termos MeSH secundário: Animais
Encéfalo/citologia
Encéfalo/embriologia
Encéfalo/metabolismo
Diferenciação Celular/fisiologia
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
MicroRNAs/genética
Neurogênese/fisiologia
Neurônios/citologia
Neurônios/metabolismo
Processamento de Proteína Pós-Traducional
Proteína EWS de Ligação a RNA/genética
Proteína EWS de Ligação a RNA/metabolismo
Proteína FUS de Ligação a RNA/genética
Proteína FUS de Ligação a RNA/metabolismo
Proteínas de Ligação a RNA/metabolismo
Fatores Associados à Proteína de Ligação a TATA/biossíntese
Fatores Associados à Proteína de Ligação a TATA/genética
Fatores Associados à Proteína de Ligação a TATA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (EWSR1 protein, human); 0 (FUS protein, human); 0 (FUS protein, mouse); 0 (MIRN141 microRNA, human); 0 (MicroRNAs); 0 (Mirn141 microRNA, mouse); 0 (RNA-Binding Protein EWS); 0 (RNA-Binding Protein FUS); 0 (RNA-Binding Proteins); 0 (TAF15 protein, human); 0 (TAF15 protein, mouse); 0 (TATA-Binding Protein Associated Factors)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180225
[Lr] Data última revisão:
180225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx160


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[PMID]:29203645
[Au] Autor:Joo YJ; Ficarro SB; Soares LM; Chun Y; Marto JA; Buratowski S
[Ad] Endereço:Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
[Ti] Título:Downstream promoter interactions of TFIID TAFs facilitate transcription reinitiation.
[So] Source:Genes Dev;31(21):2162-2174, 2017 11 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:TFIID binds promoter DNA to recruit RNA polymerase II and other basal factors for transcription. Although the TATA-binding protein (TBP) subunit of TFIID is necessary and sufficient for in vitro transcription, the TBP-associated factor (TAF) subunits recognize downstream promoter elements, act as coactivators, and interact with nucleosomes. In yeast nuclear extracts, transcription induces stable TAF binding to downstream promoter DNA, promoting subsequent activator-independent transcription reinitiation. In vivo, promoter responses to TAF mutations correlate with the level of downstream, rather than overall, Taf1 cross-linking. We propose a new model in which TAFs function as reinitiation factors, accounting for the differential responses of promoters to various transcription factor mutations.
[Mh] Termos MeSH primário: Regiões Promotoras Genéticas/fisiologia
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Fatores Associados à Proteína de Ligação a TATA/metabolismo
Transcrição Genética/genética
[Mh] Termos MeSH secundário: Acetilação
Histonas/metabolismo
Mutação/genética
Ligação Proteica
Transporte Proteico
Proteínas de Saccharomyces cerevisiae/metabolismo
Fatores Associados à Proteína de Ligação a TATA/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (BDF1 protein, S cerevisiae); 0 (Histones); 0 (Saccharomyces cerevisiae Proteins); 0 (TATA-Binding Protein Associated Factors); 0 (Transcription Factors)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1101/gad.306324.117


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[PMID]:29176831
[Au] Autor:Watanabe K; Kokubo T
[Ad] Endereço:Molecular and Cellular Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University, Yokohama, Kanagawa, Japan.
[Ti] Título:SAGA mediates transcription from the TATA-like element independently of Taf1p/TFIID but dependent on core promoter structures in Saccharomyces cerevisiae.
[So] Source:PLoS One;12(11):e0188435, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Saccharomyces cerevisiae, core promoters of class II genes contain a TATA element, either a TATA box (TATA[A/T]A[A/T][A/G]) or TATA-like element (1 or 2 bp mismatched version of the TATA box). The TATA element directs the assembly of the preinitiation complex (PIC) to ensure accurate transcriptional initiation. It has been proposed the PIC is assembled by two distinct pathways in which TBP is delivered by TFIID or SAGA, leading to the widely accepted model that these complexes mediate transcription mainly from TATA-like element- or TATA box-containing promoters, respectively. Although both complexes are involved in transcription of nearly all class II genes, it remains unclear how efficiently SAGA mediates transcription from TATA-like element-containing promoters independently of TFIID. We found that transcription from the TATA box-containing AGP1 promoter was greatly stimulated in a Spt3p-dependent manner after inactivation of Taf1p/TFIID. Thus, this promoter provides a novel experimental system in which to evaluate SAGA-mediated transcription from TATA-like element(s). We quantitatively measured transcription from various TATA-like elements in the Taf1p-dependent CYC1 promoter and Taf1p-independent AGP1 promoter. The results revealed that SAGA could mediate transcription from at least some TATA-like elements independently of Taf1p/TFIID, and that Taf1p-dependence or -independence is highly robust with respect to variation of the TATA sequence. Furthermore, chimeric promoter mapping revealed that Taf1p-dependence or independence was conferred by the upstream activating sequence (UAS), whereas Spt3p-dependent transcriptional stimulation after inactivation of Taf1p/TFIID was specific to the AGP1 promoter and dependent on core promoter regions other than the TATA box. These results suggest that TFIID and/or SAGA are regulated in two steps: the UAS first specifies TFIID or SAGA as the predominant factor on a given promoter, and then the core promoter structure guides the pertinent factor to conduct transcription in an appropriate manner.
[Mh] Termos MeSH primário: Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/genética
TATA Box/genética
Fatores Associados à Proteína de Ligação a TATA/metabolismo
Transativadores/metabolismo
Fator de Transcrição TFIID/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Sequência de Bases
Regulação Fúngica da Expressão Gênica
Genes Reporter
Cinética
Mutação/genética
Proteínas de Saccharomyces cerevisiae/genética
Fatores Associados à Proteína de Ligação a TATA/genética
Temperatura Ambiente
Fator de Transcrição TFIID/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (SAGA complex, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (TAF1 protein, S cerevisiae); 0 (TATA-Binding Protein Associated Factors); 0 (Trans-Activators); 0 (Transcription Factor TFIID)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188435


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[PMID]:28985500
[Au] Autor:Taatjes DJ
[Ad] Endereço:University of Colorado, Department of Chemistry & Biochemistry, Boulder, CO 80303, USA. Electronic address: taatjes@colorado.edu.
[Ti] Título:The Continuing SAGA of TFIID and RNA Polymerase II Transcription.
[So] Source:Mol Cell;68(1):1-2, 2017 Oct 05.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Using improved techniques, Baptista et al. (2017) and Warfield et al. (2017) revisit fundamental questions about SAGA and TFIID function in yeast. They conclude that each complex independently contributes to the expression of all genes transcribed by RNA polymerase II.
[Mh] Termos MeSH primário: RNA Polimerase II/genética
Fator de Transcrição TFIID/genética
[Mh] Termos MeSH secundário: Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Fatores Associados à Proteína de Ligação a TATA/genética
Fatores de Transcrição/genética
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); 0 (TATA-Binding Protein Associated Factors); 0 (Transcription Factor TFIID); 0 (Transcription Factors); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171007
[St] Status: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


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[PMID]:28918900
[Au] Autor:Warfield L; Ramachandran S; Baptista T; Devys D; Tora L; Hahn S
[Ad] Endereço:Fred Hutchinson Cancer Research Center, Seattle, WA 98109, USA.
[Ti] Título:Transcription of Nearly All Yeast RNA Polymerase II-Transcribed Genes Is Dependent on Transcription Factor TFIID.
[So] Source:Mol Cell;68(1):118-129.e5, 2017 Oct 05.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Previous studies suggested that expression of most yeast mRNAs is dominated by either transcription factor TFIID or SAGA. We re-examined the role of TFIID by rapid depletion of S. cerevisiae TFIID subunits and measurement of changes in nascent transcription. We find that transcription of nearly all mRNAs is strongly dependent on TFIID function. Degron-dependent depletion of Taf1, Taf2, Taf7, Taf11, and Taf13 showed similar transcription decreases for genes in the Taf1-depleted, Taf1-enriched, TATA-containing, and TATA-less gene classes. The magnitude of TFIID dependence varies with growth conditions, although this variation is similar genome-wide. Many studies have suggested differences in gene-regulatory mechanisms between TATA and TATA-less genes, and these differences have been attributed in part to differential dependence on SAGA or TFIID. Our work indicates that TFIID participates in expression of nearly all yeast mRNAs and that differences in regulation between these two gene categories is due to other properties.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica
Genoma Fúngico
RNA Polimerase II/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
Proteína de Ligação a TATA-Box/genética
Transativadores/química
Transcrição Genética
[Mh] Termos MeSH secundário: Deleção de Genes
Regiões Promotoras Genéticas
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
RNA Polimerase II/metabolismo
RNA Fúngico/genética
RNA Fúngico/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Fatores Associados à Proteína de Ligação a TATA/deficiência
Fatores Associados à Proteína de Ligação a TATA/genética
Proteína de Ligação a TATA-Box/metabolismo
Transativadores/genética
Transativadores/metabolismo
Fator de Transcrição TFIID/deficiência
Fator de Transcrição TFIID/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protein Subunits); 0 (RNA, Fungal); 0 (RNA, Messenger); 0 (SAGA complex, S cerevisiae); 0 (SPT15 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (TAF1 protein, S cerevisiae); 0 (TAF11 protein, S cerevisiae); 0 (TAF2 protein, S cerevisiae); 0 (TATA-Binding Protein Associated Factors); 0 (TATA-Box Binding Protein); 0 (Trans-Activators); 0 (Transcription Factor TFIID); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE


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[PMID]:28893950
[Au] Autor:Bardot P; Vincent SD; Fournier M; Hubaud A; Joint M; Tora L; Pourquié O
[Ad] Endereço:Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch 67400, France.
[Ti] Título:The TAF10-containing TFIID and SAGA transcriptional complexes are dispensable for early somitogenesis in the mouse embryo.
[So] Source:Development;144(20):3808-3818, 2017 10 15.
[Is] ISSN:1477-9129
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:During development, tightly regulated gene expression programs control cell fate and patterning. A key regulatory step in eukaryotic transcription is the assembly of the pre-initiation complex (PIC) at promoters. PIC assembly has mainly been studied , and little is known about its composition during development. data suggest that TFIID is the general transcription factor that nucleates PIC formation at promoters. Here we show that TAF10, a subunit of TFIID and of the transcriptional co-activator SAGA, is required for the assembly of these complexes in the mouse embryo. We performed conditional deletions during mesoderm development and show that loss in the presomitic mesoderm (PSM) does not prevent cyclic gene transcription or PSM segmental patterning, whereas lateral plate differentiation is profoundly altered. During this period, global mRNA levels are unchanged in the PSM, with only a minor subset of genes dysregulated. Together, our data strongly suggest that the TAF10-containing canonical TFIID and SAGA complexes are dispensable for early paraxial mesoderm development, arguing against the generic role in transcription proposed for these fully assembled holo-complexes.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica no Desenvolvimento
Fatores Associados à Proteína de Ligação a TATA/metabolismo
Transativadores/genética
Fator de Transcrição TFIID/genética
Transcrição Genética
[Mh] Termos MeSH secundário: Animais
Padronização Corporal
Diferenciação Celular
Núcleo Celular/metabolismo
Deleção de Genes
Mesoderma/embriologia
Mesoderma/metabolismo
Camundongos
Regiões Promotoras Genéticas
Ligação Proteica
Domínios Proteicos
RNA Mensageiro/metabolismo
Fatores Associados à Proteína de Ligação a TATA/genética
Transativadores/metabolismo
Fator de Transcrição TFIID/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (SAGA complex, mouse); 0 (TAF10 protein, mouse); 0 (TATA-Binding Protein Associated Factors); 0 (Trans-Activators); 0 (Transcription Factor TFIID)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE
[do] DOI:10.1242/dev.146902


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[PMID]:28893534
[Au] Autor:Lens Z; Cantrelle FX; Peruzzini R; Hanoulle X; Dewitte F; Ferreira E; Baert JL; Monté D; Aumercier M; Villeret V; Verger A; Landrieu I
[Ad] Endereço:UMR8576 Lille University, CNRS, F-59000 Lille, France.
[Ti] Título:Solution Structure of the N-Terminal Domain of Mediator Subunit MED26 and Molecular Characterization of Its Interaction with EAF1 and TAF7.
[So] Source:J Mol Biol;429(20):3043-3055, 2017 Oct 13.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:MED26 is a subunit of Mediator, a large complex central to the regulation of gene transcription by RNA Polymerase II. MED26 plays a role in the switch between the initiation and elongation phases of RNA Polymerase II-mediated transcription process. Regulation of these steps requires successive binding of MED26 N-terminal domain (NTD) to TATA-binding protein-associated factor 7 (TAF7) and Eleven-nineteen lysine-rich in leukemia-Associated Factor 1 (EAF1). In order to investigate the mechanism of regulation by MED26, MED26-NTD structure was solved by NMR, revealing a 4-helix bundle. EAF1 (239-268) and TAF7 (205-235) peptide interactions were both mapped to the same groove formed by H3 and H4 helices of MED26-NTD. Both interactions are characterized by dissociation constants in the 10-µM range. Further experiments revealed a folding-upon-binding mechanism that leads to the formation of EAF1 (N247-S260) and TAF7 (L214-S227) helices. Chemical shift perturbations and nuclear Overhauser enhancement contacts support the involvement of residues I222/F223 in anchoring TAF7 helix to a hydrophobic pocket of MED26-NTD, including residues L48, W80 and I84. In addition, Ala mutations of charged residues located in the C-terminal disordered part of TAF7 and EAF1 peptides affected the binding, with a loss of affinity characterized by a 10-time increase of dissociation constants. A structural model of MED26-NTD/TAF7 complex shows bi-partite components, combining ordered and disordered segments, as well as hydrophobic and electrostatic contributions to the binding. This study provides molecular detail that will help to decipher the mechanistic basis for the initiation to elongation switch-function mediated by MED26-NTD.
[Mh] Termos MeSH primário: Complexo Mediador/química
Complexo Mediador/metabolismo
Fatores Associados à Proteína de Ligação a TATA/química
Fatores Associados à Proteína de Ligação a TATA/metabolismo
Fator de Transcrição TFIID/química
Fator de Transcrição TFIID/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Seres Humanos
Espectroscopia de Ressonância Magnética
Ligação Proteica
Conformação Proteica
Mapeamento de Interação de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EAF1 protein, human); 0 (MED26 protein, human); 0 (Mediator Complex); 0 (TAF7 protein, human); 0 (TATA-Binding Protein Associated Factors); 0 (Transcription Factor TFIID); 0 (Transcription Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE


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[PMID]:28857320
[Au] Autor:Hibino E; Inoue R; Sugiyama M; Kuwahara J; Matsuzaki K; Hoshino M
[Ad] Endereço:Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto, Sakyo-ku, 606-8501, Japan.
[Ti] Título:Identification of heteromolecular binding sites in transcription factors Sp1 and TAF4 using high-resolution nuclear magnetic resonance spectroscopy.
[So] Source:Protein Sci;26(11):2280-2290, 2017 Nov.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The expression of eukaryotic genes is precisely controlled by interactions between general transcriptional factors and promoter-specific transcriptional activators. The fourth element of TATA-box binding protein-associated factor (TAF4), an essential subunit of the general transcription factor TFIID, serves as a coactivator for various promoter-specific transcriptional regulators. Interactions between TAF4 and site-specific transcriptional activators, such as Sp1, are important for regulating the expression levels of genes of interest. However, only limited information is available on the molecular mechanisms underlying the interactions between these transcriptional regulatory proteins. We herein analyzed the interaction between the transcriptional factors Sp1 and TAF4 using high-resolution solution nuclear magnetic resonance spectroscopy. We found that four glutamine-rich (Q-rich) regions in TAF4 were largely disordered under nearly physiological conditions. Among them, the first Q-rich region in TAF4 was essential for the interaction with another Q-rich region in the Sp1 molecule, most of which was largely disordered. The residues responsible for this interaction were specific and highly localized in a defined region within a range of 20-30 residues. Nevertheless, a detailed analysis of C-chemical shift values suggested that no significant conformational change occurred upon binding. These results indicate a prominent and exceptional binding mode for intrinsically disordered proteins other than the well-accepted concept of "coupled folding and binding."
[Mh] Termos MeSH primário: Proteínas Intrinsicamente Desordenadas/química
Fator de Transcrição Sp1/química
Fatores Associados à Proteína de Ligação a TATA/química
Fator de Transcrição TFIID/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sítios de Ligação
Isótopos de Carbono
Seres Humanos
Proteínas Intrinsicamente Desordenadas/metabolismo
Isótopos de Nitrogênio
Ressonância Magnética Nuclear Biomolecular/métodos
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Fator de Transcrição Sp1/metabolismo
Fatores Associados à Proteína de Ligação a TATA/metabolismo
Fator de Transcrição TFIID/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carbon Isotopes); 0 (Intrinsically Disordered Proteins); 0 (Nitrogen Isotopes); 0 (Recombinant Proteins); 0 (Sp1 Transcription Factor); 0 (Sp1 protein, human); 0 (TAF4 protein, human); 0 (TATA-Binding Protein Associated Factors); 0 (Transcription Factor TFIID)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3287


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[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



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