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  1 / 9625 MEDLINE  
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[PMID]:29422501
[Au] Autor:Collopy LC; Ware TL; Goncalves T; Í Kongsstovu S; Yang Q; Amelina H; Pinder C; Alenazi A; Moiseeva V; Pearson SR; Armstrong CA; Tomita K
[Ad] Endereço:Chromosome Maintenance Group, UCL Cancer Institute, University College London, London, WC1E 6DD, UK.
[Ti] Título:LARP7 family proteins have conserved function in telomerase assembly.
[So] Source:Nat Commun;9(1):557, 2018 02 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Understanding the intricacies of telomerase regulation is crucial due to the potential health benefits of modifying its activity. Telomerase is composed of an RNA component and reverse transcriptase. However, additional factors required during biogenesis vary between species. Here we have identified fission yeast Lar7 as a member of the conserved LARP7 family, which includes the Tetrahymena telomerase-binding protein p65 and human LARP7. We show that Lar7 has conserved RNA-recognition motifs, which bind telomerase RNA to protect it from exosomal degradation. In addition, Lar7 is required to stabilise the association of telomerase RNA with the protective complex LSm2-8, and telomerase reverse transcriptase. Lar7 remains a component of the mature telomerase complex and is required for telomerase localisation to the telomere. Collectively, we demonstrate that Lar7 is a crucial player in fission yeast telomerase biogenesis, similarly to p65 in Tetrahymena, and highlight the LARP7 family as a conserved factor in telomere maintenance.
[Mh] Termos MeSH primário: Proteínas Nucleares/genética
Fosfoproteínas/genética
Proteínas de Protozoários/genética
RNA Fúngico/genética
DNA Polimerase Dirigida por RNA/genética
RNA/genética
Ribonucleoproteínas/genética
Schizosaccharomyces/genética
Telomerase/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência Conservada
Expressão Gênica
Seres Humanos
Isoenzimas/genética
Isoenzimas/metabolismo
Proteínas Nucleares/metabolismo
Fosfoproteínas/metabolismo
Ligação Proteica
Proteínas de Protozoários/metabolismo
RNA/metabolismo
Estabilidade de RNA
RNA Fúngico/metabolismo
DNA Polimerase Dirigida por RNA/metabolismo
Ribonucleoproteínas/metabolismo
Schizosaccharomyces/metabolismo
Telomerase/metabolismo
Telômero/química
Telômero/ultraestrutura
Tetrahymena thermophila/genética
Tetrahymena thermophila/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Larp7 protein, human); 0 (Nuclear Proteins); 0 (Pdd1 protein, Tetrahymena); 0 (Phosphoproteins); 0 (Protozoan Proteins); 0 (RNA, Fungal); 0 (Ribonucleoproteins); 0 (Ter1 telomerase subunit, S pombe); 63231-63-0 (RNA); EC 2.7.7.49 (RNA-Directed DNA Polymerase); EC 2.7.7.49 (Telomerase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180307
[Lr] Data última revisão:
180307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180210
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02296-4


  2 / 9625 MEDLINE  
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[PMID]:28746974
[Au] Autor:Sheinberger J; Shav-Tal Y
[Ad] Endereço:The Mina & Everard Goodman Faculty of Life Sciences, Institute of Nanotechnology, Bar-Ilan University, Ramat Gan, Israel.
[Ti] Título:mRNPs meet stress granules.
[So] Source:FEBS Lett;591(17):2534-2542, 2017 09.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Stress granules are cytoplasmic structures that form in response to a variety of cellular stresses. They contain mRNAs and many proteins including numerous types of RNA-binding proteins, and have been studied in connection to major cellular events such as protein synthesis as well as disease. Despite the well-known fact that stress granules encapsulate mRNPs (mRNA-protein complexes), much of the research has naturally focused on the protein components of stress granules. The specific details of mRNP entry into and exit from stress granules and the functional reasons for these dynamics are not fully understood. Here, we review studies that have concentrated on the aspects of mRNP accumulation in stress granules and produced quantitative data concerning mRNP/stress granule interactions.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/metabolismo
Ribonucleoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Doença/genética
Seres Humanos
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Ribonucleoproteins); 0 (messenger ribonucleoprotein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12765


  3 / 9625 MEDLINE  
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[PMID]:29269694
[Au] Autor:Matsui T; Nakagawa K; Yamazaki K; Wada T; Kadoya M; Kaida K
[Ad] Endereço:Department of Neurology, Anti-aging and Vascular Medicine, National Defense Medical College.
[Ti] Título:[An anti-RNP antibody-positive case of aseptic meningitis induced by non-steroidal anti-inflammatory drugs in a young woman].
[So] Source:Rinsho Shinkeigaku;58(1):25-29, 2018 Jan 26.
[Is] ISSN:1882-0654
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:A 19-year-old woman developed high fever, headache, and nausea after taking Loxoprofen for pharyngitis, followed by disturbed consciousness and nuchal stiffness. The patient and her mother had a history of Raynaud's phenomenon. Cerebrospinal fluid (CSF) examination indicated a diagnosis of aseptic meningitis and revealed high levels of Q albumin and IgG index. Anti-RNP antibodies were positive in serum and CSF. Her symptoms disappeared immediately after cessation of Loxoprofen and a drug lymphocyte stimulation test was negative, confirming a diagnosis of non-steroidal anti-inflammatory drugs (NSAIDs)-induced aseptic meningitis. It should be kept in mind that an immune abnormality such as serum and CSF anti-RNP antibodies may play a role in development of NSAIDs-induced aseptic meningitis. A history of usage of NSAIDs and a thorough examination of collagen diseases are useful for identification of the origin of aseptic meningitis in a young woman.
[Mh] Termos MeSH primário: Anti-Inflamatórios não Esteroides/efeitos adversos
Anticorpos Antinucleares/sangue
Anticorpos Antinucleares/líquido cefalorraquidiano
Meningite Asséptica/diagnóstico
Meningite Asséptica/etiologia
Fenilpropionatos/efeitos adversos
Ribonucleoproteínas/imunologia
[Mh] Termos MeSH secundário: Acetaminofen/administração & dosagem
Adulto
Anti-Inflamatórios não Esteroides/administração & dosagem
Doenças Autoimunes/complicações
Doenças Autoimunes/diagnóstico
Autoimunidade
Biomarcadores/sangue
Biomarcadores/líquido cefalorraquidiano
Diagnóstico Diferencial
Substituição de Medicamentos
Feminino
Seres Humanos
Resultado do Tratamento
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Antibodies, Antinuclear); 0 (Biomarkers); 0 (Phenylpropionates); 0 (Ribonucleoproteins); 3583H0GZAP (loxoprofen); 362O9ITL9D (Acetaminophen)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.5692/clinicalneurol.cn-001085


  4 / 9625 MEDLINE  
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[PMID]:29366779
[Au] Autor:Fukumura K; Inoue K; Mayeda A
[Ad] Endereço:Division of Gene Expression Mechanism, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake 470-1192, Aichi, Japan.
[Ti] Título:Splicing activator RNPS1 suppresses errors in pre-mRNA splicing: A key factor for mRNA quality control.
[So] Source:Biochem Biophys Res Commun;496(3):921-926, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human RNPS1 protein was first identified as a pre-mRNA splicing activator in vitro and RNPS1 regulates alternative splicing in cellulo. RNPS1 was also known as a peripheral factor of the exon junction complex (EJC). Here we show that cellular knockdown of RNPS1 induced a reduction of the wild-type aurora kinase B (AURKB) protein due to the induced aberrant pre-mRNA splicing events, indicating that the fidelity of AURKB pre-mRNA splicing was reduced. The major aberrant AURKB mRNA was derived from the upstream pseudo 5' and 3' splice sites in intron 5, which resulted in the production of the non-functional truncated AURKB protein. AURKB, is an essential mitotic factor, whose absence is known to cause multiple nuclei, and this multinucleation phenotype was recapitulated in RNPS1-knockdown cells. Importantly this RNPS1-knockdown phenotype was rescued by ectopic expression of AURKB, implying it is a major functional target of RNPS1. We found RNPS1 protein, not as a component of the EJC, binds directly to a specific element in the AURKB exon upstream of the authentic 5' splice site, and this binding is required for normal splicing. RNPS1-knockdown induces a parallel aberrant splicing pattern in a fully distinct pre-mRNA, MDM2, suggesting that RNPS1 is a global guardian of splicing fidelity. We conclude that RNPS1 is a key factor for the quality control of mRNAs that is essential for the phenotypes including cell division.
[Mh] Termos MeSH primário: Aurora Quinase B/genética
Genes Supressores
Precursores de RNA/genética
Processamento de RNA/genética
RNA Mensageiro/genética
Ribonucleoproteínas/genética
[Mh] Termos MeSH secundário: Células HeLa
Seres Humanos
Controle de Qualidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA Precursors); 0 (RNA, Messenger); 0 (RNPS1 protein, human); 0 (Ribonucleoproteins); EC 2.7.11.1 (AURKB protein, human); EC 2.7.11.1 (Aurora Kinase B)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


  5 / 9625 MEDLINE  
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[PMID]:29358748
[Au] Autor:Kucherenko MM; Shcherbata HR
[Ad] Endereço:Max Planck Research Group of Gene Expression and Signaling, Max Planck Institute for Biophysical Chemistry, Am Fassberg, 11, Goettingen, 37077, Germany.
[Ti] Título:Stress-dependent miR-980 regulation of Rbfox1/A2bp1 promotes ribonucleoprotein granule formation and cell survival.
[So] Source:Nat Commun;9(1):312, 2018 01 22.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Upon stress, profound post-transcriptional adjustments of gene expression occur in spatially restricted, subcellular, membraneless compartments, or ribonucleoprotein (RNP) granules, which are formed by liquid phase separation of RNA-binding proteins with low complexity sequence domains (LCDs). Here, we show that Rbfox1 is an LCD-containing protein that aggregates into liquid droplets and amyloid-like fibers and promiscuously joins different nuclear and cytoplasmic RNP granules. Using Drosophila oogenesis as an in vivo system for stress response, we demonstrate a mechanism by which Rbfox1 promotes cell survival. The stress-dependent miRNA miR-980 acts to buffer Rbfox1 levels, since it targets only those Rbfox1 transcripts that contain extended 3'UTRs. Reduced miR-980 expression during stress leads to increased Rbfox1 levels, widespread formation of various RNP granules, and increased cell viability. We show that human RBFOX proteins also contain multiple LCDs and form membraneless compartments, suggesting that the RNP granule-linked control of cellular adaptive responses may contribute to a wide range of RBFOX-associated pathologies in humans.
[Mh] Termos MeSH primário: Proteínas de Drosophila/genética
MicroRNAs/genética
Oócitos/metabolismo
Proteínas de Ligação a RNA/genética
Ribonucleoproteínas/genética
Estresse Fisiológico/genética
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Animais
Sobrevivência Celular
Reprogramação Celular
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/genética
Drosophila melanogaster/crescimento & desenvolvimento
Drosophila melanogaster/metabolismo
Feminino
Fibroblastos/citologia
Fibroblastos/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Seres Humanos
MicroRNAs/metabolismo
Mutação
Neurônios/citologia
Neurônios/metabolismo
Oócitos/citologia
Oogênese/genética
Ovário/citologia
Ovário/metabolismo
Cultura Primária de Células
Domínios Proteicos
Proteínas de Ligação a RNA/metabolismo
Ribonucleoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (MicroRNAs); 0 (RNA-Binding Proteins); 0 (Rbfox1 protein, Drosophila); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180124
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02757-w


  6 / 9625 MEDLINE  
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[PMID]:29274781
[Au] Autor:Liu D; Qian W; Li D; Kong L
[Ad] Endereço:Department of Gastroenteology and Hepatology, The First Affiliated Hospital of Zhengzhou University, Zhengzhou, 450052, China. Electronic address: danliu666@hotmail.com.
[Ti] Título:Ro60/SSA levels are increased and promote the progression of pancreatic ductal adenocarcinoma.
[So] Source:Biochem Biophys Res Commun;495(4):2519-2524, 2018 01 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ro60/SSA is a vital auto antigen that is targeted in Sjogren's syndrome and systemic lupus erythematosus (SLE). However, its role in solid cancers has rarely been reported. The present study investigated the expression and function of Ro60/SSA in the development of pancreatic ductal adenocarcinoma (PDAC) both in vitro and in vivo. Immunohistochemistry was used to examine the expression of Ro60/SSA in PDAC and normal pancreatic tissues by using tissue microarray chips. The results showed that Ro60/SSA expression was increased in PDAC tissues compared with normal pancreatic tissues. Knockdown of Ro60/SSA by siRNA transfection significantly decreased cell proliferation and invasion in vitro. Furthermore, knockdown of Ro60/SSA inhibited the growth of subcutaneous tumors in vivo. Taken together, the current study provides evidence of new function of Ro60/SSA in the development of cancer. It facilitates pancreatic cancer proliferation, migration and invasion. Therefore, it may represent a novel molecular target for the management of pancreatic cancer.
[Mh] Termos MeSH primário: Autoantígenos/metabolismo
Carcinoma Ductal Pancreático/metabolismo
Carcinoma Ductal Pancreático/patologia
Neoplasias Pancreáticas/metabolismo
Neoplasias Pancreáticas/patologia
RNA Citoplasmático Pequeno/metabolismo
Ribonucleoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Proliferação Celular
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Nus
Invasividade Neoplásica
Células Tumorais Cultivadas
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantigens); 0 (RNA, Small Cytoplasmic); 0 (Ribonucleoproteins); 0 (TROVE2 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171225
[St] Status:MEDLINE


  7 / 9625 MEDLINE  
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[PMID]:28467905
[Au] Autor:Ramdzan YM; Trubetskov MM; Ormsby AR; Newcombe EA; Sui X; Tobin MJ; Bongiovanni MN; Gras SL; Dewson G; Miller JML; Finkbeiner S; Moily NS; Niclis J; Parish CL; Purcell AW; Baker MJ; Wilce JA; Waris S; Stojanovski D; Böcking T; Ang CS; Ascher DB; Reid GE; Hatters DM
[Ad] Endereço:Department of Biochemistry and Molecular Biology and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, VIC 3010, Australia.
[Ti] Título:Huntingtin Inclusions Trigger Cellular Quiescence, Deactivate Apoptosis, and Lead to Delayed Necrosis.
[So] Source:Cell Rep;19(5):919-927, 2017 May 02.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Competing models exist in the literature for the relationship between mutant Huntingtin exon 1 (Httex1) inclusion formation and toxicity. In one, inclusions are adaptive by sequestering the proteotoxicity of soluble Httex1. In the other, inclusions compromise cellular activity as a result of proteome co-aggregation. Using a biosensor of Httex1 conformation in mammalian cell models, we discovered a mechanism that reconciles these competing models. Newly formed inclusions were composed of disordered Httex1 and ribonucleoproteins. As inclusions matured, Httex1 reconfigured into amyloid, and other glutamine-rich and prion domain-containing proteins were recruited. Soluble Httex1 caused a hyperpolarized mitochondrial membrane potential, increased reactive oxygen species, and promoted apoptosis. Inclusion formation triggered a collapsed mitochondrial potential, cellular quiescence, and deactivated apoptosis. We propose a revised model where sequestration of soluble Httex1 inclusions can remove the trigger for apoptosis but also co-aggregate other proteins, which curtails cellular metabolism and leads to a slow death by necrosis.
[Mh] Termos MeSH primário: Amiloide/metabolismo
Apoptose
Proteína Huntingtina/genética
[Mh] Termos MeSH secundário: Éxons
Células HEK293
Células HeLa
Seres Humanos
Proteína Huntingtina/metabolismo
Corpos de Inclusão/metabolismo
Potencial da Membrana Mitocondrial
Mutação
Espécies Reativas de Oxigênio/metabolismo
Ribonucleoproteínas/genética
Ribonucleoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid); 0 (HTT protein, human); 0 (Huntingtin Protein); 0 (Reactive Oxygen Species); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  8 / 9625 MEDLINE  
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[PMID]:27773663
[Au] Autor:Lenart M; Rutkowska-Zapala M; Szatanek R; Weglarczyk K; Stec M; Bukowska-Strakova K; Gruca A; Czyz J; Siedlar M
[Ad] Endereço:Department of Clinical Immunology, Institute of Paediatrics, Faculty of Medicine, Jagiellonian University Medical College, Krakow, Poland.
[Ti] Título:Alterations of TRIM21-mRNA expression during monocyte maturation.
[So] Source:Immunobiology;222(3):494-498, 2017 03.
[Is] ISSN:1878-3279
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Tripartite motif-containing protein 21 (TRIM21) play a dual role in the cytoplasm of the cells where it facilitates destruction of some antibody-coated viruses and some bacteria, and initiates synthesis of proinflammatory cytokines. Macrophages and CD16 monocyte subset can particularly participate in a proinflammatory response caused by viral infection, however, the molecular mechanisms underlying these processes are not fully understood. The aim of this study was to determine the level of TRIM21-mRNA expression in monocyte subsets including: classical (CD14 CD16 ), intermediate (CD14 CD16 ) and non-classical (CD14 CD16 ) monocytes, as well as during in vitro differentiation of the isolated monocytes towards dendritic cells or macrophages. Our results revealed that the level of TRIM21 mRNA expression was significantly lower in CD16- monocytes, when compared to CD16 cells and the whole monocyte population, yet no significant differences were observed when CD16 population was divided into intermediate and non-classical subsets. More pronounced differences were observed in the case of monocyte-derived macrophages (MDM) and dendritic cells (DCs). TRIM21-mRNA expression level was app. 6-fold higher in DCs, and app. 16-fold higher in MDM (p<0,01), when compared to freshly isolated monocytes. Our results may suggest the new mechanism of increased proinflammatory cytokine production by CD16 (intermediate and non-classical) monocytes and macrophages, at least in patients with acute or chronic infections, caused by enveloped viruses. We suggest that TRIM21 may be one of the factors associated with the "switching on" the proinflammatory programme in CD16 monocytes or monocyte-derived macrophages.
[Mh] Termos MeSH primário: Diferenciação Celular/genética
Regulação da Expressão Gênica
Monócitos/citologia
Monócitos/metabolismo
Ribonucleoproteínas/genética
[Mh] Termos MeSH secundário: Adulto
Biomarcadores
Diferenciação Celular/imunologia
Células Dendríticas/imunologia
Células Dendríticas/metabolismo
Feminino
Seres Humanos
Imunofenotipagem
Macrófagos/citologia
Macrófagos/imunologia
Macrófagos/metabolismo
Masculino
Meia-Idade
Monócitos/imunologia
Fenótipo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ribonucleoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); 0 (RNA, Messenger); 0 (Ribonucleoproteins); 0 (SS-A antigen)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  9 / 9625 MEDLINE  
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[PMID]:29302061
[Au] Autor:Noda T; Murakami S; Nakatsu S; Imai H; Muramoto Y; Shindo K; Sagara H; Kawaoka Y
[Ad] Endereço:Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8639, Japan. t-noda@infront.kyoto-u.ac.jp.
[Ti] Título:Importance of the 1+7 configuration of ribonucleoprotein complexes for influenza A virus genome packaging.
[So] Source:Nat Commun;9(1):54, 2018 01 04.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The influenza A virus genome is composed of eight single-stranded negative-sense RNAs. Eight distinct viral RNA segments (vRNAs) are selectively packaged into progeny virions, with eight vRNAs in ribonucleoprotein complexes (RNPs) arranged in a specific "1+7" pattern, that is, one central RNP surrounded by seven RNPs. Here we report the genome packaging of an artificially generated seven-segment virus that lacks the hemagglutinin (HA) vRNA. Electron microscopy shows that, even in the presence of only seven vRNAs, the virions efficiently package eight RNPs arranged in the same "1+7" pattern as wild-type virions. Next-generation sequencing reveals that the virions specifically incorporate host-derived 18S and 28S ribosomal RNAs (rRNAs) seemingly as the eighth RNP in place of the HA vRNA. These findings highlight the importance of the assembly of eight RNPs into a specific "1+7" configuration for genome packaging in progeny virions and suggest a potential role for cellular RNAs in viral genome packaging.
[Mh] Termos MeSH primário: Genoma Viral
Vírus da Influenza A/genética
Ribonucleoproteínas/metabolismo
Montagem de Vírus
[Mh] Termos MeSH secundário: Regulação Viral da Expressão Gênica/fisiologia
Células HEK293
Seres Humanos
RNA Viral/genética
Ribonucleoproteínas/química
Ribonucleoproteínas/genética
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Viral); 0 (Ribonucleoproteins); 0 (Viral Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180106
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02517-w


  10 / 9625 MEDLINE  
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[PMID]:29261807
[Au] Autor:Khamina K; Lercher A; Caldera M; Schliehe C; Vilagos B; Sahin M; Kosack L; Bhattacharya A; Májek P; Stukalov A; Sacco R; James LC; Pinschewer DD; Bennett KL; Menche J; Bergthaler A
[Ad] Endereço:CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse, Vienna, Austria.
[Ti] Título:Characterization of host proteins interacting with the lymphocytic choriomeningitis virus L protein.
[So] Source:PLoS Pathog;13(12):e1006758, 2017 Dec.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNA-dependent RNA polymerases (RdRps) play a key role in the life cycle of RNA viruses and impact their immunobiology. The arenavirus lymphocytic choriomeningitis virus (LCMV) strain Clone 13 provides a benchmark model for studying chronic infection. A major genetic determinant for its ability to persist maps to a single amino acid exchange in the viral L protein, which exhibits RdRp activity, yet its functional consequences remain elusive. To unravel the L protein interactions with the host proteome, we engineered infectious L protein-tagged LCMV virions by reverse genetics. A subsequent mass-spectrometric analysis of L protein pulldowns from infected human cells revealed a comprehensive network of interacting host proteins. The obtained LCMV L protein interactome was bioinformatically integrated with known host protein interactors of RdRps from other RNA viruses, emphasizing interconnected modules of human proteins. Functional characterization of selected interactors highlighted proviral (DDX3X) as well as antiviral (NKRF, TRIM21) host factors. To corroborate these findings, we infected Trim21-/- mice with LCMV and found impaired virus control in chronic infection. These results provide insights into the complex interactions of the arenavirus LCMV and other viral RdRps with the host proteome and contribute to a better molecular understanding of how chronic viruses interact with their host.
[Mh] Termos MeSH primário: RNA Helicases DEAD-box/metabolismo
Vírus da Coriomeningite Linfocítica/enzimologia
Modelos Moleculares
RNA Replicase/metabolismo
Proteínas Repressoras/metabolismo
Ribonucleoproteínas/metabolismo
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Animais
Sistemas CRISPR-Cas
Biologia Computacional
Cruzamentos Genéticos
RNA Helicases DEAD-box/química
Feminino
Células HEK293
Seres Humanos
Imunoprecipitação
Coriomeningite Linfocítica/metabolismo
Coriomeningite Linfocítica/veterinária
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Domínios e Motivos de Interação entre Proteínas
RNA Replicase/química
RNA Replicase/genética
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Repressoras/química
Ribonucleoproteínas/química
Ribonucleoproteínas/genética
Organismos Livres de Patógenos Específicos
Proteínas Virais/química
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (NKRF protein, human); 0 (Recombinant Fusion Proteins); 0 (Repressor Proteins); 0 (Ribonucleoproteins); 0 (SS-A antigen); 0 (Viral Proteins); EC 2.7.7.48 (RNA Replicase); EC 3.6.1.- (DDX3X protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180109
[Lr] Data última revisão:
180109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006758



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