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  1 / 6913 MEDLINE  
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[PMID]:29414693
[Au] Autor:Andreev DE; Dmitriev SE; Loughran G; Terenin IM; Baranov PV; Shatsky IN
[Ad] Endereço:Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia. Electronic address: cycloheximide@yandex.ru.
[Ti] Título:Translation control of mRNAs encoding mammalian translation initiation factors.
[So] Source:Gene;651:174-182, 2018 Apr 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Eukaryotic cells evolved highly complex and accurate protein synthesis machinery that is finely tuned by various signaling pathways. Dysregulation of translation is a hallmark of many diseases, including cancer, and thus pharmacological approaches to modulate translation become very promising. While there has been much progress in our understanding of mammalian mRNA-specific translation control, surprisingly, relatively little is known about whether and how the protein components of the translation machinery shape translation of their own mRNAs. Here we analyze mammalian mRNAs encoding components of the translation initiation machinery for potential regulatory features such as 5'TOP motifs, TISU motifs, poor start codon nucleotide context and upstream open reading frames.
[Mh] Termos MeSH primário: Fatores de Iniciação em Eucariotos/genética
Regulação da Expressão Gênica
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Animais
Seres Humanos
Mamíferos
Biossíntese de Proteínas
Sequência de Oligopirimidina na Região 5' Terminal do RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Eukaryotic Initiation Factors); 0 (RNA, Messenger)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180208
[St] Status:MEDLINE


  2 / 6913 MEDLINE  
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[PMID]:29351555
[Au] Autor:Xue Y; Chen B; Win AN; Fu C; Lian J; Liu X; Wang R; Zhang X; Chai Y
[Ad] Endereço:College of Agronomy and Biotechnology, Southwest University, Chongqing, China.
[Ti] Título:Omega-3 fatty acid desaturase gene family from two ω-3 sources, Salvia hispanica and Perilla frutescens: Cloning, characterization and expression.
[So] Source:PLoS One;13(1):e0191432, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Omega-3 fatty acid desaturase (ω-3 FAD, D15D) is a key enzyme for α-linolenic acid (ALA) biosynthesis. Both chia (Salvia hispanica) and perilla (Perilla frutescens) contain high levels of ALA in seeds. In this study, the ω-3 FAD gene family was systematically and comparatively cloned from chia and perilla. Perilla FAD3, FAD7, FAD8 and chia FAD7 are encoded by single-copy (but heterozygous) genes, while chia FAD3 is encoded by 2 distinct genes. Only 1 chia FAD8 sequence was isolated. In these genes, there are 1 to 6 transcription start sites, 1 to 8 poly(A) tailing sites, and 7 introns. The 5'UTRs of PfFAD8a/b contain 1 to 2 purine-stretches and 2 pyrimidine-stretches. An alternative splice variant of ShFAD7a/b comprises a 5'UTR intron. Their encoded proteins harbor an FA_desaturase conserved domain together with 4 trans-membrane helices and 3 histidine boxes. Phylogenetic analysis validated their identity of dicot microsomal or plastidial ω-3 FAD proteins, and revealed some important evolutionary features of plant ω-3 FAD genes such as convergent evolution across different phylums, single-copy status in algae, and duplication events in certain taxa. The qRT-PCR assay showed that the ω-3 FAD genes of two species were expressed at different levels in various organs, and they also responded to multiple stress treatments. The functionality of the ShFAD3 and PfFAD3 enzymes was confirmed by yeast expression. The systemic molecular and functional features of the ω-3 FAD gene family from chia and perilla revealed in this study will facilitate their use in future studies on genetic improvement of ALA traits in oilseed crops.
[Mh] Termos MeSH primário: Ácidos Graxos Dessaturases/genética
Genes de Plantas
Perilla frutescens/enzimologia
Perilla frutescens/genética
Proteínas de Plantas/genética
Salvia/enzimologia
Salvia/genética
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Processamento Alternativo
Sequência de Aminoácidos
Clonagem Molecular
Sequência Conservada
Evolução Molecular
Ácidos Graxos Dessaturases/química
Ácidos Graxos Dessaturases/metabolismo
Regulação Enzimológica da Expressão Gênica
Regulação da Expressão Gênica de Plantas
Família Multigênica
Especificidade de Órgãos
Filogenia
Proteínas de Plantas/química
Proteínas de Plantas/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA de Plantas/genética
RNA de Plantas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Estresse Fisiológico
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Plant Proteins); 0 (RNA, Messenger); 0 (RNA, Plant); 0 (Recombinant Proteins); EC 1.14.19.- (Fatty Acid Desaturases); EC 1.14.99.- (omega-3 fatty acid desaturase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191432


  3 / 6913 MEDLINE  
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[PMID]:28457784
[Au] Autor:Vandenbussche F; Lefebvre DJ; De Leeuw I; Van Borm S; De Clercq K
[Ad] Endereço:Molecular Platform, OD Viral Diseases, CODA-CERVA, Groeselenberg 99, 1180 Brussels, Belgium.
[Ti] Título:Laboratory validation of two real-time RT-PCR methods with 5'-tailed primers for an enhanced detection of foot-and-mouth disease virus.
[So] Source:J Virol Methods;246:90-94, 2017 Aug.
[Is] ISSN:1879-0984
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The 3D and 5UTR real-time RT-PCR assays (RT-qPCR) from Callahan et al. (2002) and Reid et al. (2002) are commonly used reference methods for the detection of foot-and-mouth disease virus (FMDV). For an optimal detection of FMDV in clinical samples, it is advised to use both assays simultaneously (King et al., 2006). Recently, Vandenbussche et al. (2016) showed that the addition of 5'-tails to the FMDV-specific primers enhances the detection of FMDV in both the 3D and the 5UTR RT-qPCR assay. To validate the 3D and 5UTR RT-qPCR assays with 5'-tailed primers for diagnostic purposes, both assays were run in parallel in a triplex one-step RT-qPCR protocol with beta-actin as an internal control and synthetic RNA as an external control. We obtained low limits of detection and high linearity's, high repeatability and reproducibility, near 100% analytical specificity and >99% diagnostic accuracy for both assays. It was concluded that the 3D and 5UTR RT-qPCR assays with 5'-tailed primers are particularly suited for the detection of FMDV as well as to exclude the presence of FMDV.
[Mh] Termos MeSH primário: Regiões 5´ não Traduzidas
Primers do DNA
Vírus da Febre Aftosa/isolamento & purificação
Febre Aftosa/diagnóstico
Reação em Cadeia da Polimerase Via Transcriptase Reversa/métodos
[Mh] Termos MeSH secundário: Animais
Febre Aftosa/virologia
Vírus da Febre Aftosa/genética
RNA Viral/sangue
RNA Viral/genética
Reprodutibilidade dos Testes
Sensibilidade e Especificidade
Ovinos/virologia
Suínos/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (DNA Primers); 0 (RNA, Viral)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  4 / 6913 MEDLINE  
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[PMID]:28743463
[Au] Autor:Rivas-Aravena A; Muñoz P; Jorquera P; Diaz A; Reinoso C; González-Catrilelbún S; Sandino AM
[Ad] Endereço:Comisión Chilena de Energía Nuclear, Departamento de Aplicaciones Nucleares, Laboratorio de Radiobiología Celular y Molecular. Nueva Bilbao 12501, Las Condes, Santiago, Chile; Universidad San Sebastián, Facultad de Ciencias, Lota 2465, Providencia, Santiago, Chile. Electronic address: andrea.rivas@c
[Ti] Título:Study of RNA-A Initiation Translation of The Infectious Pancreatic Necrosis Virus.
[So] Source:Virus Res;240:121-129, 2017 08 15.
[Is] ISSN:1872-7492
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The infectious pancreatic necrosis virus (IPNV) is a salmonid pathogen that causes significant economic losses to the aquaculture industry. IPNV is a non-enveloped virus containing two uncapped and non-polyadenylated double strand RNA genomic segments, RNA-A and RNA-B. The viral protein Vpg is covalently attached to the 5' end of both segments. There is little knowledge about its viral cycle, particularly about the translation of the RNAs. Through experiments using mono and bicistronic reporters, in this work we show that the 120-nucleotide-long 5'-UTR of RNA-A contains an internal ribosome entry site (IRES) that functions efficiently both in vitro and in salmon cells. IRES activity is strongly dependent on temperature. Also, the IRES structure is confined to the 5'UTR and is not affected by the viral coding sequence. This is the first report of IRES activity in a fish virus and can give us tools to generate antivirals to attack the virus without affecting fish directly.
[Mh] Termos MeSH primário: Infecções por Birnaviridae/veterinária
Doenças dos Peixes/virologia
Vírus da Necrose Pancreática Infecciosa/genética
Biossíntese de Proteínas
RNA Viral/genética
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Animais
Infecções por Birnaviridae/virologia
Regulação Viral da Expressão Gênica
Vírus da Necrose Pancreática Infecciosa/química
Vírus da Necrose Pancreática Infecciosa/metabolismo
Sítios Internos de Entrada Ribossomal
Conformação de Ácido Nucleico
RNA Mensageiro/química
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Viral/química
RNA Viral/metabolismo
Ribossomos/genética
Ribossomos/metabolismo
Salmo salar
Proteínas Virais/genética
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Internal Ribosome Entry Sites); 0 (RNA, Messenger); 0 (RNA, Viral); 0 (Viral Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE


  5 / 6913 MEDLINE  
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[PMID]:29287083
[Au] Autor:Manee MM; Alharbi SN; Algarni AT; Alghamdi WM; Altammami MA; Alkhrayef MN; Alnafjan BM
[Ad] Endereço:National Center for Genomic Technology, King Abdulaziz City for Science and Technology, Riyadh, Saudi Arabia.
[Ti] Título:Molecular cloning, bioinformatics analysis, and expression of small heat shock protein beta-1 from Camelus dromedarius, Arabian camel.
[So] Source:PLoS One;12(12):e0189905, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Small heat shock protein beta-1 (HSPB-1) plays an essential role in the protection of cells against environmental stress.Elucidation of its molecular, structural, and biological characteristics in a naturally wild-type model is essential. Although the sequence information of the HSPB-1 gene is available for many mammalian species, the HSPB-1 gene of Arabian camel (Arabian camel HSPB-1) has not yet been structurally characterized. We cloned and functionally characterized a full-length of Arabian camel HSPB-1 cDNA. It is 791 bp long, with a 5'-untranslated region (UTR) of 34 bp, a 3'-UTR of 151 bp with a poly(A) tail, and an open reading frame (ORF) of 606 bp encoding a protein of 201 amino acids (accession number: MF278354). The tissue-specific expression analysis of Arabian camel HSPB-1 mRNA was examined using quantitative real-time PCR (qRT-PCR); which suggested that Arabian camel HSPB-1 mRNA was constitutionally expressed in all examined tissues of Arabian camel, with the predominately level in the esophagus tissue. Peptide mass fingerprint-mass spectrometry (PMF-MS) analysis of the purified Arabian camel HSPB-1 protein confirmed the identity of this protein. Phylogenetic analysis showed that the HSPB-1 protein of Arabian camel is grouped together with those of Bactrian camel and Alpaca. Comparing the modelled 3D structure of Arabian camel HSPB-1 protein with the available protein 3D structure of HSPB-1 from human confirmed the presence of α-crystallin domain, and high similarities were noted between the two structures by using super secondary structure prediction.
[Mh] Termos MeSH primário: Camelus/genética
Biologia Computacional
Proteínas de Choque Térmico/genética
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Sequência de Aminoácidos
Animais
Cromatografia Líquida
Clonagem Molecular
DNA Complementar/genética
Expressão Gênica
Proteínas de Choque Térmico/química
Modelos Moleculares
Filogenia
Estrutura Secundária de Proteína
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
Homologia de Sequência de Aminoácidos
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (DNA, Complementary); 0 (Heat-Shock Proteins); 0 (RNA, Messenger)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189905


  6 / 6913 MEDLINE  
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[PMID]:28450395
[Au] Autor:Zhang Q; Meng X; Li D; Chen S; Luo J; Zhu L; Singer RH; Gu W
[Ad] Endereço:From the Department of Pathophysiology, Key Immunopathology Laboratory of Guangdong Province, Shantou University Medical College, Shantou, Guangdong Province 515031, China and.
[Ti] Título:Binding of DEAD-box helicase Dhh1 to the 5'-untranslated region of mRNA represses localized translation of in yeast cells.
[So] Source:J Biol Chem;292(23):9787-9800, 2017 06 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Local translation of specific mRNAs is regulated by dynamic changes in their subcellular localization, and these changes are due to complex mechanisms controlling cytoplasmic mRNA transport. The budding yeast is well suited to studying these mechanisms because many of its transcripts are transported from the mother cell to the budding daughter cell. Here, we investigated the translational control of mRNA after transport and localization. We show that although transcripts were translated after they reached the bud tip, some mRNAs were bound by the RNA-binding protein Puf6 and were non-polysomal. We also found that the DEAD-box helicase Dhh1 complexed with the untranslated mRNA and Puf6. Loss of Dhh1 affected local translation of mRNA and resulted in delocalization of transcript in the bud. Forcibly shifting the non-polysomal mRNA into polysomes was associated with Dhh1 dissociation. We further demonstrated that Dhh1 is not recruited to mRNA co-transcriptionally, suggesting that it could bind to mRNA within the cytoplasm. Of note, Dhh1 bound to the 5'-UTR of mRNA and inhibited its translation These results suggest that after localization to the bud tip, a portion of the localized mRNA becomes translationally inactive because of binding of Dhh1 and Puf6 to the 5'- and 3'-UTRs of mRNA.
[Mh] Termos MeSH primário: Regiões 5´ não Traduzidas/fisiologia
RNA Helicases DEAD-box/metabolismo
Biossíntese de Proteínas/fisiologia
RNA Fúngico/metabolismo
Proteínas Repressoras/biossíntese
Proteínas de Saccharomyces cerevisiae/biossíntese
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: RNA Helicases DEAD-box/genética
RNA Fúngico/genética
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Proteínas Repressoras/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (ASH1 protein, S cerevisiae); 0 (Puf6 protein, S cerevisiae); 0 (RNA, Fungal); 0 (RNA-Binding Proteins); 0 (Repressor Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (DHH1 protein, S cerevisiae); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1706
[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.M117.776492


  7 / 6913 MEDLINE  
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[PMID]:29216274
[Au] Autor:Bruno W; Andreotti V; Bisio A; Pastorino L; Fornarini G; Sciallero S; Bianchi-Scarrà G; Inga A; Ghiorzo P
[Ad] Endereço:Genetics of Rare Cancers, Department of Internal Medicine and Medical Specialties (DiMI), University of Genoa and Ospedale Policlinico San Martino, Genoa, Italy.
[Ti] Título:Functional analysis of a CDKN2A 5'UTR germline variant associated with pancreatic cancer development.
[So] Source:PLoS One;12(12):e0189123, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CDKN2A coding region germline variants are associated with pancreatic adenocarcinoma (PC) susceptibility. Recently, we described functional germline 5'UTR CDKN2A variants from melanoma patients affecting the post-transcriptional regulation of p16INK4a mRNA that is dependent, at least in part, on an Internal Ribosome Entry Site (IRES) in the 5'UTR region. Here we describe a 5'UTR c.-201_-198delinsCTTT CDKN2A variant (frequency 0.0028 based on 350 PC patients), which seems to be private to PC, since it has never been found in public databases nor in thousands of melanoma patients tested. Functional analyses confirmed IRES activity of the 5'UTR in BX-PC3 PC cells and revealed a functional impact of the identified variant. Using gene reporter assays we observed reduced translation potential in cells treated with the mTOR inhibitor Torin1, a condition that favors the assessment of IRES activity. At the endogenous gene level we quantified allelic imbalance among polysome-associated mRNAs using a patient-derived cell line heterozygous for the c.-201_-198delinsCTTT. Overall, we conclude that this very rare private variant can be considered a potential mutation, specifically associated with PC. Our data indicate that sequencing of the entire 5'UTR of CDKN2A should be included in routine screening of PC cases with suspected inherited susceptibility.
[Mh] Termos MeSH primário: Regiões 5´ não Traduzidas
Mutação em Linhagem Germinativa
Neoplasias Pancreáticas/genética
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Masculino
Linhagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5' Untranslated Regions)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189123


  8 / 6913 MEDLINE  
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[PMID]:28468879
[Au] Autor:Foscaldi S; D'Antuono A; Noval MG; de Prat Gay G; Scolaro L; Lopez N
[Ad] Endereço:Centro de Virología Animal, Instituto de Ciencia y Tecnología Dr. Cesar Milstein, Consejo Nacional de Ciencia y Tecnología, Buenos Aires, Argentina.
[Ti] Título:Regulation of Tacaribe Mammarenavirus Translation: Positive 5' and Negative 3' Elements and Role of Key Cellular Factors.
[So] Source:J Virol;91(14), 2017 Jul 15.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammarenaviruses are enveloped viruses with a bisegmented negative-stranded RNA genome that encodes the nucleocapsid protein (NP), the envelope glycoprotein precursor (GPC), the RNA polymerase (L), and a RING matrix protein (Z). Viral proteins are synthesized from subgenomic mRNAs bearing a capped 5' untranslated region (UTR) and lacking 3' poly(A) tail. We analyzed the translation strategy of Tacaribe virus (TCRV), a prototype of the New World mammarenaviruses. A virus-like transcript that carries a reporter gene in place of the NP open reading frame and transcripts bearing modified 5' and/or 3' UTR were evaluated in a cell-based translation assay. We found that the presence of the cap structure at the 5' end dramatically increases translation efficiency and that the viral 5' UTR comprises stimulatory signals while the 3' UTR,specifically the presence of a terminal C+G-rich sequence and/or a stem-loop structure, down-modulates translation. Additionally, translation was profoundly reduced in eukaryotic initiation factor (eIF) 4G-inactivated cells, whereas depletion of intracellular levels of eIF4E had less impact on virus-like mRNA translation than on a cell-like transcript. Translation efficiency was independent of NP expression or TCRV infection. Our results indicate that TCRV mRNAs are translated using a cap-dependent mechanism, whose efficiency relies on the interplay between stimulatory signals in the 5' UTR and a negative modulatory element in the 3' UTR. The low dependence on eIF4E suggests that viral mRNAs may engage yet-unknown noncanonical host factors for a cap-dependent initiation mechanism. Several members of the family cause serious hemorrhagic fevers in humans. In the present report, we describe the mechanism by which Tacaribe virus, a prototypic nonpathogenic New World mammarenavirus, regulates viral mRNA translation. Our results highlight the impact of untranslated sequences and key host translation factors on this process. We propose a model that explains how viral mRNAs outcompete cellular mRNAs for the translation machinery. A better understanding of the mechanism of translation regulation of this virus can provide the bases for the rational design of new antiviral tools directed to pathogenic arenaviruses.
[Mh] Termos MeSH primário: Regiões 3´ não Traduzidas/genética
Regiões 5´ não Traduzidas/genética
Arenavirus do Novo Mundo/genética
Regulação Viral da Expressão Gênica
Biossíntese de Proteínas
RNA Mensageiro/genética
Sequências Reguladoras de Ácido Ribonucleico
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Fator de Iniciação 4E em Eucariotos/metabolismo
Fator de Iniciação 4G em Eucariotos/metabolismo
Interações Hospedeiro-Patógeno
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (5' Untranslated Regions); 0 (Eukaryotic Initiation Factor-4E); 0 (Eukaryotic Initiation Factor-4G); 0 (RNA, Messenger); 0 (Regulatory Sequences, Ribonucleic Acid)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  9 / 6913 MEDLINE  
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[PMID]:28456022
[Au] Autor:Biegel JM; Henderson E; Cox EM; Bonenfant G; Netzband R; Kahn S; Eager R; Pager CT
[Ad] Endereço:Department of Biological Sciences, The RNA Institute, University at Albany-SUNY, Albany, NY 12222, USA.
[Ti] Título:Cellular DEAD-box RNA helicase DDX6 modulates interaction of miR-122 with the 5' untranslated region of hepatitis C virus RNA.
[So] Source:Virology;507:231-241, 2017 07.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hepatitis C virus (HCV) subverts the cellular DEAD-box RNA helicase DDX6 to promote virus infection. Using polysome gradient analysis and the subgenomic HCV Renilla reporter replicon genome, we determined that DDX6 does not affect HCV translation. Rather expression of the subgenomic HCV Renilla luciferase reporter at late times, as well as labeling of newly synthesized viral RNA with 4-thiouridine showed that DDX6 modulates replication. Because DDX6 is an effector protein of the microRNA pathway, we also investigated its role in miR-122-directed HCV gene expression. Similar to sequestering miR-122, depletion of DDX6 modulated HCV RNA stability. Interestingly, miR-122-HCV RNA interaction assays with mutant HCV genomes sites and compensatory exogenous miR-122 showed that DDX6 affects the function of miR-122 at one particular binding site. We propose that DDX6 facilitates the miR-122 interaction with HCV 5' UTR, which is necessary for stabilizing the viral genome and the switch between translation and replication.
[Mh] Termos MeSH primário: RNA Helicases DEAD-box/metabolismo
Hepacivirus/metabolismo
Hepatite C/enzimologia
MicroRNAs/metabolismo
Proteínas Proto-Oncogênicas/metabolismo
RNA Viral/metabolismo
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Linhagem Celular Tumoral
RNA Helicases DEAD-box/genética
Hepacivirus/genética
Hepatite C/genética
Hepatite C/metabolismo
Hepatite C/virologia
Seres Humanos
MicroRNAs/genética
Proteínas Proto-Oncogênicas/genética
RNA Viral/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 (5' Untranslated Regions); 0 (MIRN122 microRNA, human); 0 (MicroRNAs); 0 (Proto-Oncogene Proteins); 0 (RNA, Viral); EC 3.6.1.- (DDX6 protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


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[PMID]:28459542
[Au] Autor:Warden MS; Tonelli M; Cornilescu G; Liu D; Hopersberger LJ; Ponniah K; Pascal SM
[Ad] Endereço:Department of Chemistry and Biochemistry, Old Dominion University , Norfolk, Virginia 23529, United States.
[Ti] Título:Structure of RNA Stem Loop B from the Picornavirus Replication Platform.
[So] Source:Biochemistry;56(20):2549-2557, 2017 05 23.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The presumptive RNA cloverleaf at the start of the 5'-untranslated region of the picornavirus genome is an essential element in replication. Stem loop B (SLB) of the cloverleaf is a recognition site for the host polyC-binding protein, which initiates a switch from translation to replication. Here we present the solution structure of human rhinovirus isotype 14 SLB using nuclear magnetic resonance spectroscopy. SLB adopts a predominantly A-form helical structure. The stem contains five Watson-Crick base pairs and one wobble base pair and is capped by an eight-nucleotide loop. The wobble base pair introduces perturbations into the helical parameters but does not appear to introduce flexibility. However, the helix major groove appears to be accessible. Flexibility is seen throughout the loop and in the terminal nucleotides. The pyrimidine-rich region of the loop, the apparent recognition site for the polyC-binding protein, is the most disordered region of the structure.
[Mh] Termos MeSH primário: Conformação de Ácido Nucleico
Picornaviridae/fisiologia
RNA Viral/química
Replicação Viral
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Picornaviridae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (RNA, Viral)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171205
[Lr] Data última revisão:
171205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00141



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