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Pesquisa : D12.776.157.725.750.750 [Categoria DeCS]
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  1 / 110 MEDLINE  
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[PMID]:28934473
[Au] Autor:Yeh CS; Chang SL; Chen JH; Wang HK; Chou YC; Wang CH; Huang SH; Larson A; Pleiss JA; Chang WH; Chang TH
[Ad] Endereço:Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei, Taiwan.
[Ti] Título:The conserved AU dinucleotide at the 5' end of nascent U1 snRNA is optimized for the interaction with nuclear cap-binding-complex.
[So] Source:Nucleic Acids Res;45(16):9679-9693, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Splicing is initiated by a productive interaction between the pre-mRNA and the U1 snRNP, in which a short RNA duplex is established between the 5' splice site of a pre-mRNA and the 5' end of the U1 snRNA. A long-standing puzzle has been why the AU dincucleotide at the 5'-end of the U1 snRNA is highly conserved, despite the absence of an apparent role in the formation of the duplex. To explore this conundrum, we varied this AU dinucleotide into all possible permutations and analyzed the resulting molecular consequences. This led to the unexpected findings that the AU dinucleotide dictates the optimal binding of cap-binding complex (CBC) to the 5' end of the nascent U1 snRNA, which ultimately influences the utilization of U1 snRNP in splicing. Our data also provide a structural interpretation as to why the AU dinucleotide is conserved during evolution.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Cap de RNA/metabolismo
RNA Nuclear Pequeno/química
RNA Nuclear Pequeno/metabolismo
[Mh] Termos MeSH secundário: Pareamento de Bases
Simulação de Acoplamento Molecular
Complexo Proteico Nuclear de Ligação ao Cap/genética
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Proteínas de Ligação ao Cap de RNA/genética
Precursores de RNA/metabolismo
Processamento de RNA
RNA Nuclear Pequeno/genética
Ribonucleoproteína Nuclear Pequena U1/genética
Ribonucleoproteína Nuclear Pequena U1/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Leveduras/genética
Leveduras/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CBC2 protein, S cerevisiae); 0 (Nuclear Cap-Binding Protein Complex); 0 (RNA Cap-Binding Proteins); 0 (RNA Precursors); 0 (RNA, Small Nuclear); 0 (Ribonucleoprotein, U1 Small Nuclear); 0 (Saccharomyces cerevisiae Proteins); 0 (U1 small nuclear RNA)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx608


  2 / 110 MEDLINE  
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[PMID]:28934468
[Au] Autor:Shi M; Zhang H; Wu X; He Z; Wang L; Yin S; Tian B; Li G; Cheng H
[Ad] Endereço:State Key Laboratory of Molecular Biology, Shanghai Key Laboratory of Molecular Andrology, CAS Center for Excellence in Molecular Cell Science, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China.
[Ti] Título:ALYREF mainly binds to the 5' and the 3' regions of the mRNA in vivo.
[So] Source:Nucleic Acids Res;45(16):9640-9653, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The TREX complex (TREX) plays key roles in nuclear export of mRNAs. However, little is known about its transcriptome-wide binding targets. We used individual cross-linking and immunoprecipitation (iCLIP) to identify the binding sites of ALYREF, an mRNA export adaptor in TREX, in human cells. Consistent with previous in vitro studies, ALYREF binds to a region near the 5' end of the mRNA in a CBP80-dependent manner. Unexpectedly, we identified PABPN1-dependent ALYREF binding near the 3' end of the mRNA. Furthermore, the 3' processing factor CstF64 directly interacts with ALYREF and is required for the overall binding of ALYREF on the mRNA. In addition, we found that numerous middle exons harbor ALYREF binding sites and identified ALYREF-binding motifs that promote nuclear export of intronless mRNAs. Together, our study defines enrichment of ALYREF binding sites at the 5' and the 3' regions of the mRNA in vivo, identifies export-promoting ALYREF-binding motifs, and reveals CstF64- and PABPN1-mediated coupling of mRNA nuclear export to 3' processing.
[Mh] Termos MeSH primário: Proteínas Nucleares/metabolismo
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Fator Estimulador de Clivagem/genética
Fator Estimulador de Clivagem/metabolismo
Células HeLa
Seres Humanos
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Proteínas Nucleares/genética
Proteína I de Ligação a Poli(A)/metabolismo
Transporte de RNA
RNA Mensageiro/química
Proteínas de Ligação a RNA/genética
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ALYREF protein, human); 0 (Cleavage Stimulation Factor); 0 (Nuclear Cap-Binding Protein Complex); 0 (Nuclear Proteins); 0 (PABPN1 protein, human); 0 (Poly(A)-Binding Protein I); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Transcription Factors)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx597


  3 / 110 MEDLINE  
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[PMID]:28858511
[Au] Autor:Okon A; Han J; Dawadi S; Demosthenous C; Aldrich CC; Gupta M; Wagner CR
[Ti] Título:Anchimerically Activated ProTides as Inhibitors of Cap-Dependent Translation and Inducers of Chemosensitization in Mantle Cell Lymphoma.
[So] Source:J Med Chem;60(19):8131-8144, 2017 Oct 12.
[Is] ISSN:1520-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cellular delivery of nucleotides through various pronucleotide strategies has expanded the utility of nucleosides as a therapeutic class. Although highly successful, the highly popular ProTide system relies on a four-step enzymatic and chemical process to liberate the corresponding monophosphate. To broaden the scope and reduce the number of steps required for monophosphate release, we have developed a strategy that depends on initial chemical activation by a sulfur atom of a methylthioalkyl protecting group, followed by enzymatic hydrolysis of the resulting phosphoramidate monoester. We have employed this ProTide strategy for intracellular delivery of a nucleotide antagonist of eIF4E in mantle cell lymphoma (MCL) cells. Furthermore, we demonstrated that chemical inhibition of cap-dependent translation results in suppression of c-Myc expression, increased p27 expression, and enhanced chemosensitization to doxorubicin, dexamethasone, and ibrutinib. In addition, the new ProTide strategy was shown to enhance oral bioavailability of the corresponding monoester phosphoramidate.
[Mh] Termos MeSH primário: Antineoplásicos/síntese química
Antineoplásicos/farmacologia
Linfoma de Célula do Manto/tratamento farmacológico
Complexo Proteico Nuclear de Ligação ao Cap/efeitos dos fármacos
Peptídeos/síntese química
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacocinética
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Inibidor de Quinase Dependente de Ciclina p27/antagonistas & inibidores
Inibidor de Quinase Dependente de Ciclina p27/biossíntese
Desenho de Drogas
Fator de Iniciação 4E em Eucariotos/antagonistas & inibidores
Feminino
Seres Humanos
Linfoma de Célula do Manto/patologia
Proteínas Proto-Oncogênicas c-myc/antagonistas & inibidores
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Eukaryotic Initiation Factor-4E); 0 (Nuclear Cap-Binding Protein Complex); 0 (Peptides); 0 (Proto-Oncogene Proteins c-myc); 147604-94-2 (Cyclin-Dependent Kinase Inhibitor p27)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170901
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jmedchem.7b00916


  4 / 110 MEDLINE  
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[PMID]:28064320
[Au] Autor:Popova VV; Glukhova AA; Georgieva SG; Georgiev GP; Kopytova DV
[Ad] Endereço:Institute of Gene Biology, Russian Academy of Sciences, Moscow, 119334 Russia.
[Ti] Título:[Interactions of the TREX-2 complex with mRNP particle of ß-tubulin 56D gene].
[So] Source:Mol Biol (Mosk);50(6):1030-1038, 2016 Nov-Dec.
[Is] ISSN:0026-8984
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:mRNA transport from the nucleus to the cytoplasm is an essential step of eukaryotic gene expression. A pre-mRNA molecule undergoes modification, such as 5'-capping, splicing, and 3'-end processing, in the nucleus. The molecule being modified interacts with a large number of proteins and, thus, mRNP particles are formed. The binding of factors involved in nuclear export also occurs during transcription and mRNA processing. We have shown that the functioning of TREX-2, an mRNA export complex, is restricted to the nucleus. We used the method of RNA coprecipitation that enables the selective extraction of RNA-protein complexes from samples to show that the transcription elongation complex TREX interacts with mRNA of the ß-tubulin 56D gene over the entire length of the molecule. The capping protein Cbp80 reacted both with the cap structure and with a specific part of the coding mRNA of the ß-tubulin 56D gene. The TREX-2 complex that mediates mRNA export from the nucleus to the cytoplasm is bound to the same part of the coding sequence. Thus, we identified a common binding site for all of the complexes under investigation on the mRNA of ß-tubulin 56D. Co-immunoprecipitation reactions performed with S2 cell extracts revealed interactions between the components of complexes involved in transcription elongation, maturation, and export of mRNA. The model of molecular folding for the mRNP particle involving the mRNA of ß-tubulin 56D has been proposed.
[Mh] Termos MeSH primário: Modelos Biológicos
Complexos Multiproteicos/metabolismo
RNA Mensageiro/metabolismo
Ribonucleoproteínas/metabolismo
Elongação da Transcrição Genética/fisiologia
Tubulina (Proteína)/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Proteínas de Drosophila/genética
Proteínas de Drosophila/metabolismo
Drosophila melanogaster
Complexos Multiproteicos/genética
Complexo Proteico Nuclear de Ligação ao Cap/genética
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
RNA Mensageiro/genética
Ribonucleoproteínas/genética
Tubulina (Proteína)/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cbp80 protein, Drosophila); 0 (Drosophila Proteins); 0 (Multiprotein Complexes); 0 (Nuclear Cap-Binding Protein Complex); 0 (RNA, Messenger); 0 (Ribonucleoproteins); 0 (Tubulin); 0 (messenger ribonucleoprotein)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170321
[Lr] Data última revisão:
170321
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170109
[St] Status:MEDLINE
[do] DOI:10.7868/S002689841606015X


  5 / 110 MEDLINE  
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[PMID]:27758893
[Au] Autor:Yu X; Willmann MR; Anderson SJ; Gregory BD
[Ad] Endereço:Department of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104.
[Ti] Título:Genome-Wide Mapping of Uncapped and Cleaved Transcripts Reveals a Role for the Nuclear mRNA Cap-Binding Complex in Cotranslational RNA Decay in Arabidopsis.
[So] Source:Plant Cell;28(10):2385-2397, 2016 Oct.
[Is] ISSN:1532-298X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNA turnover is necessary for controlling proper mRNA levels posttranscriptionally. In general, RNA degradation is via exoribonucleases that degrade RNA either from the 5' end to the 3' end, such as XRN4, or in the opposite direction by the multisubunit exosome complex. Here, we use genome-wide mapping of uncapped and cleaved transcripts to reveal the global landscape of cotranslational mRNA decay in the Arabidopsis thaliana transcriptome. We found that this process leaves a clear three nucleotide periodicity in open reading frames. This pattern of cotranslational degradation is especially evident near the ends of open reading frames, where we observe accumulation of cleavage events focused 16 to 17 nucleotides upstream of the stop codon because of ribosomal pausing during translation termination. Following treatment of Arabidopsis plants with the translation inhibitor cycloheximide, cleavage events accumulate 13 to 14 nucleotides upstream of the start codon where initiating ribosomes have been stalled with these sequences in their P site. Further analysis in xrn4 mutant plants indicates that cotranslational RNA decay is XRN4 dependent. Additionally, studies in plants lacking CAP BINDING PROTEIN80/ABA HYPERSENSITIVE1, the largest subunit of the nuclear mRNA cap binding complex, reveal a role for this protein in cotranslational decay. In total, our results demonstrate the global prevalence and features of cotranslational RNA decay in a plant transcriptome.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Arabidopsis/genética
Arabidopsis/metabolismo
Estabilidade de RNA/genética
RNA Mensageiro/genética
[Mh] Termos MeSH secundário: Arabidopsis/efeitos dos fármacos
Cicloeximida/farmacologia
Exorribonucleases/genética
Exorribonucleases/metabolismo
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Regulação da Expressão Gênica de Plantas/genética
Complexo Proteico Nuclear de Ligação ao Cap/genética
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Estabilidade de RNA/fisiologia
RNA de Plantas/genética
Ribossomos/genética
Ribossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Nuclear Cap-Binding Protein Complex); 0 (Plant Proteins); 0 (RNA, Messenger); 0 (RNA, Plant); 0 (Xrn1 protein, plant); 98600C0908 (Cycloheximide); EC 3.1.- (Exoribonucleases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161021
[St] Status:MEDLINE


  6 / 110 MEDLINE  
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[PMID]:26773052
[Au] Autor:Gromadzka AM; Steckelberg AL; Singh KK; Hofmann K; Gehring NH
[Ad] Endereço:Institute for Genetics, University of Cologne, D-50674 Cologne, Germany.
[Ti] Título:A short conserved motif in ALYREF directs cap- and EJC-dependent assembly of export complexes on spliced mRNAs.
[So] Source:Nucleic Acids Res;44(5):2348-61, 2016 Mar 18.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The export of messenger RNAs (mRNAs) is the final of several nuclear posttranscriptional steps of gene expression. The formation of export-competent mRNPs involves the recruitment of export factors that are assumed to facilitate transport of the mature mRNAs. Using in vitro splicing assays, we show that a core set of export factors, including ALYREF, UAP56 and DDX39, readily associate with the spliced RNAs in an EJC (exon junction complex)- and cap-dependent manner. In order to elucidate how ALYREF and other export adaptors mediate mRNA export, we conducted a computational analysis and discovered four short, conserved, linear motifs present in RNA-binding proteins. We show that mutation in one of the new motifs (WxHD) in an unstructured region of ALYREF reduced RNA binding and abolished the interaction with eIF4A3 and CBP80. Additionally, the mutation impaired proper localization to nuclear speckles and export of a spliced reporter mRNA. Our results reveal important details of the orchestrated recruitment of export factors during the formation of export competent mRNPs.
[Mh] Termos MeSH primário: Sequência Conservada
Proteínas Nucleares/genética
Processamento de RNA
RNA Mensageiro/genética
Proteínas de Ligação a RNA/genética
Ribonucleoproteínas/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Transporte Biológico
Clonagem Molecular
RNA Helicases DEAD-box/genética
RNA Helicases DEAD-box/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Fator de Iniciação 4A em Eucariotos/genética
Fator de Iniciação 4A em Eucariotos/metabolismo
Éxons
Expressão Gênica
Células HEK293
Células HeLa
Seres Humanos
Dados de Sequência Molecular
Mutação
Complexo Proteico Nuclear de Ligação ao Cap/genética
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Proteínas Nucleares/metabolismo
Ligação Proteica
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ribonucleoproteínas/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ALYREF protein, human); 0 (Nuclear Cap-Binding Protein Complex); 0 (Nuclear Proteins); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Recombinant Proteins); 0 (Ribonucleoproteins); 0 (Transcription Factors); 0 (messenger ribonucleoprotein); EC 2.7.7.- (Eukaryotic Initiation Factor-4A); EC 3.6.1.- (DDX39A protein, human); EC 3.6.1.- (DDX39B protein, human); EC 3.6.1.- (EIF4A3 protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160322
[Lr] Data última revisão:
160322
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160117
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw009


  7 / 110 MEDLINE  
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[PMID]:26382858
[Au] Autor:Gebhardt A; Habjan M; Benda C; Meiler A; Haas DA; Hein MY; Mann A; Mann M; Habermann B; Pichlmair A
[Ad] Endereço:Innate Immunity Laboratory, Max-Planck Institute of Biochemistry, Martinsried, Munich D-82152, Germany.
[Ti] Título:mRNA export through an additional cap-binding complex consisting of NCBP1 and NCBP3.
[So] Source:Nat Commun;6:8192, 2015 Sep 18.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The flow of genetic information from DNA to protein requires polymerase-II-transcribed RNA characterized by the presence of a 5'-cap. The cap-binding complex (CBC), consisting of the nuclear cap-binding protein (NCBP) 2 and its adaptor NCBP1, is believed to bind all capped RNA and to be necessary for its processing and intracellular localization. Here we show that NCBP1, but not NCBP2, is required for cell viability and poly(A) RNA export. We identify C17orf85 (here named NCBP3) as a cap-binding protein that together with NCBP1 forms an alternative CBC in higher eukaryotes. NCBP3 binds mRNA, associates with components of the mRNA processing machinery and contributes to poly(A) RNA export. Loss of NCBP3 can be compensated by NCBP2 under steady-state conditions. However, NCBP3 becomes pivotal under stress conditions, such as virus infection. We propose the existence of an alternative CBC involving NCBP1 and NCBP3 that plays a key role in mRNA biogenesis.
[Mh] Termos MeSH primário: Complexo Proteico Nuclear de Ligação ao Cap/genética
Proteínas de Ligação ao Cap de RNA/genética
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Animais
Sobrevivência Celular
Cercopithecus aethiops
Cromatografia Líquida
Imunofluorescência
Técnicas de Silenciamento de Genes
Células HeLa
Seres Humanos
Imunoprecipitação
Hibridização in Situ Fluorescente
Macrófagos/metabolismo
Camundongos
Células NIH 3T3
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Proteínas de Ligação ao Cap de RNA/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Espectrometria de Massas em Tandem
Células Vero
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nuclear Cap-Binding Protein Complex); 0 (RNA Cap-Binding Proteins); 0 (RNA, Messenger)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150919
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms9192


  8 / 110 MEDLINE  
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[PMID]:26303529
[Au] Autor:O'Sullivan C; Christie J; Pienaar M; Gambling J; Nickerson PE; Alford SC; Chow RL; Howard PL
[Ad] Endereço:Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
[Ti] Título:Mutagenesis of ARS2 Domains To Assess Possible Roles in Cell Cycle Progression and MicroRNA and Replication-Dependent Histone mRNA Biogenesis.
[So] Source:Mol Cell Biol;35(21):3753-67, 2015 Nov.
[Is] ISSN:1098-5549
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ARS2 is a regulator of RNA polymerase II transcript processing through its role in the maturation of distinct nuclear cap-binding complex (CBC)-controlled RNA families. In this study, we examined ARS2 domain function in transcript processing. Structural modeling based on the plant ARS2 orthologue, SERRATE, revealed 2 previously uncharacterized domains in mammalian ARS2: an N-terminal domain of unknown function (DUF3546), which is also present in SERRATE, and an RNA recognition motif (RRM) that is present in metazoan ARS2 but not in plants. Both the DUF3546 and zinc finger domain (ZnF) were required for association with microRNA and replication-dependent histone mRNA. Mutations in the ZnF disrupted interaction with FLASH, a key component in histone pre-mRNA processing. Mutations targeting the Mid domain implicated it in DROSHA interaction and microRNA biogenesis. The unstructured C terminus was required for interaction with the CBC protein CBP20, while the RRM was required for cell cycle progression and for binding to FLASH. Together, our results support a bridging model in which ARS2 plays a central role in RNA recognition and processing through multiple protein and RNA interactions.
[Mh] Termos MeSH primário: Ciclo Celular
Histonas/genética
MicroRNAs/genética
Proteínas Nucleares/metabolismo
RNA Mensageiro/genética
Fatores de Transcrição/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas de Ligação ao Cálcio/metabolismo
Células Cultivadas
Histonas/metabolismo
Camundongos Endogâmicos C57BL
MicroRNAs/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
Mutagênese
Complexo Proteico Nuclear de Ligação ao Cap
Proteínas Nucleares/química
Proteínas Nucleares/genética
Estrutura Terciária de Proteína
RNA Mensageiro/metabolismo
Fase S
Fatores de Transcrição/química
Fatores de Transcrição/genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Ars2 protein, mouse); 0 (Calcium-Binding Proteins); 0 (Casp8ap2 protein, mouse); 0 (Histones); 0 (MicroRNAs); 0 (Nuclear Cap-Binding Protein Complex); 0 (Nuclear Proteins); 0 (RNA, Messenger); 0 (Transcription Factors)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:160501
[Lr] Data última revisão:
160501
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150826
[St] Status:MEDLINE
[do] DOI:10.1128/MCB.00272-15


  9 / 110 MEDLINE  
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[PMID]:26048019
[Au] Autor:Zhang Y; Sachs MS
[Ad] Endereço:Department of Biology, Texas A&M University, College Station, Texas 77843-3258.
[Ti] Título:Control of mRNA Stability in Fungi by NMD, EJC and CBC Factors Through 3'UTR Introns.
[So] Source:Genetics;200(4):1133-48, 2015 Aug.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In higher eukaryotes the accelerated degradation of mRNAs harboring premature termination codons is controlled by nonsense-mediated mRNA decay (NMD), exon junction complex (EJC), and nuclear cap-binding complex (CBC) factors, but the mechanistic basis for this quality-control system and the specific roles of the individual factors remain unclear. Using Neurospora crassa as a model system, we analyzed the mechanisms by which NMD is induced by spliced 3'-UTR introns or upstream open reading frames and observed that the former requires NMD, EJC, and CBC factors whereas the latter requires only the NMD factors. The transcripts for EJC components eIF4A3 and Y14, and translation termination factor eRF1, contain spliced 3'-UTR introns and each was stabilized in NMD, EJC, and CBC mutants. Reporter mRNAs containing spliced 3'-UTR introns, but not matched intronless controls, were stabilized in these mutants and were enriched in mRNPs immunopurified from wild-type cells with antibody directed against human Y14, demonstrating a direct role for spliced 3'-UTR introns in triggering EJC-mediated NMD. These results demonstrate conclusively that NMD, EJC, and CBC factors have essential roles in controlling mRNA stability and that, based on differential requirements for these factors, there are branched mechanisms for NMD. They demonstrate for the first time autoregulatory control of expression at the level of mRNA stability through the EJC/CBC branch of NMD for EJC core components, eIF4A3 and Y14, and for eRF1, which recognizes termination codons. Finally, these results show that EJC-mediated NMD occurs in fungi and thus is an evolutionarily conserved quality-control mechanism.
[Mh] Termos MeSH primário: Regiões 3´ não Traduzidas/genética
Códon sem Sentido/metabolismo
Proteínas Fúngicas/metabolismo
Íntrons/genética
Neurospora crassa/genética
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Estabilidade de RNA
[Mh] Termos MeSH secundário: Seres Humanos
Mutação
Neurospora crassa/metabolismo
Fases de Leitura Aberta/genética
Precursores de RNA/química
Precursores de RNA/genética
Precursores de RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Codon, Nonsense); 0 (Fungal Proteins); 0 (Nuclear Cap-Binding Protein Complex); 0 (RNA Precursors)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150607
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.115.176743


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[PMID]:25049393
[Au] Autor:Kroczynska B; Mehrotra S; Majchrzak-Kita B; Arslan AD; Altman JK; Stein BL; McMahon B; Kozlowski P; Kahle PJ; Eklund EA; Fish EN; Platanias LC
[Ad] Endereço:Robert H. Lurie Comprehensive Cancer Center andDivision of Hematology/Oncology, Northwestern University Medical School, Chicago, IL 60611;
[Ti] Título:Regulatory effects of SKAR in interferon α signaling and its role in the generation of type I IFN responses.
[So] Source:Proc Natl Acad Sci U S A;111(31):11377-82, 2014 Aug 05.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We provide evidence that S6 kinase 1 (S6K1) Aly/REF-like target (SKAR) is engaged in IFN-α signaling and plays a key role in the generation of IFN responses. Our data demonstrate that IFN-α induces phosphorylation of SKAR, which is mediated by either the p90 ribosomal protein S6 kinase (RSK) or p70 S6 kinase (S6K1), in a cell type-specific manner. This type I IFN-inducible phosphorylation of SKAR results in enhanced interaction with the eukaryotic initiation factor (eIF)4G and recruitment of activated RSK1 to 5' cap mRNA. Our studies also establish that SKAR is present in cap-binding CBP80 immune complexes and that this interaction is mediated by eIF4G. We demonstrate that inducible protein expression of key IFN-α-regulated protein products such as ISG15 and p21(WAF1/CIP1) requires SKAR activity. Importantly, our studies define a requirement for SKAR in the generation of IFN-α-dependent inhibitory effects on malignant hematopoietic progenitors from patients with chronic myeloid leukemia or myeloproliferative neoplasms. Taken altogether, these findings establish critical and essential roles for SKAR in the regulation of mRNA translation of IFN-sensitive genes and induction of IFN-α biological responses.
[Mh] Termos MeSH primário: Interferon-alfa/metabolismo
Proteínas Nucleares/metabolismo
Proteínas de Ligação a RNA/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Linhagem Celular Tumoral
Inibidor de Quinase Dependente de Ciclina p21/metabolismo
Citocinas/metabolismo
Guanosina/análogos & derivados
Guanosina/metabolismo
Seres Humanos
Camundongos
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Fosforilação/efeitos dos fármacos
Proteínas Quinases S6 Ribossômicas 90-kDa/metabolismo
Transdução de Sinais/efeitos dos fármacos
Ubiquitinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Cyclin-Dependent Kinase Inhibitor p21); 0 (Cytokines); 0 (Interferon-alpha); 0 (Nuclear Cap-Binding Protein Complex); 0 (Nuclear Proteins); 0 (POLDIP3 protein, human); 0 (RNA-Binding Proteins); 0 (Ubiquitins); 12133JR80S (Guanosine); 2140-77-4 (7-methylguanosine); 60267-61-0 (ISG15 protein, human); EC 2.7.11.1 (Ribosomal Protein S6 Kinases, 90-kDa)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140723
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1405250111



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