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[PMID]:27903772
[Au] Autor:Pocock GM; Zimdars LL; Yuan M; Eliceiri KW; Ahlquist P; Sherer NM
[Ad] Endereço:McArdle Laboratory for Cancer Research and Institute for Molecular Virology, University of Wisconsin-Madison, Madison, WI 53706.
[Ti] Título:Diverse activities of viral cis-acting RNA regulatory elements revealed using multicolor, long-term, single-cell imaging.
[So] Source:Mol Biol Cell;28(3):476-487, 2017 Feb 01.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cis-acting RNA structural elements govern crucial aspects of viral gene expression. How these structures and other posttranscriptional signals affect RNA trafficking and translation in the context of single cells is poorly understood. Herein we describe a multicolor, long-term (>24 h) imaging strategy for measuring integrated aspects of viral RNA regulatory control in individual cells. We apply this strategy to demonstrate differential mRNA trafficking behaviors governed by RNA elements derived from three retroviruses (HIV-1, murine leukemia virus, and Mason-Pfizer monkey virus), two hepadnaviruses (hepatitis B virus and woodchuck hepatitis virus), and an intron-retaining transcript encoded by the cellular NXF1 gene. Striking behaviors include "burst" RNA nuclear export dynamics regulated by HIV-1's Rev response element and the viral Rev protein; transient aggregations of RNAs into discrete foci at or near the nuclear membrane triggered by multiple elements; and a novel, pulsiform RNA export activity regulated by the hepadnaviral posttranscriptional regulatory element. We incorporate single-cell tracking and a data-mining algorithm into our approach to obtain RNA element-specific, high-resolution gene expression signatures. Together these imaging assays constitute a tractable, systems-based platform for studying otherwise difficult to access spatiotemporal features of viral and cellular gene regulation.
[Mh] Termos MeSH primário: Imagem Molecular/métodos
Análise de Célula Única/métodos
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular/fisiologia
Núcleo Celular/metabolismo
Regulação Viral da Expressão Gênica
Produtos do Gene rev/metabolismo
Genes env/fisiologia
HIV-1
Vírus dos Macacos de Mason-Pfizer
Processamento Pós-Transcricional do RNA/fisiologia
RNA Mensageiro/metabolismo
RNA Viral
Sequências Reguladoras de Ácido Nucleico/genética
Sequências Reguladoras de Ácido Nucleico/fisiologia
Sequências Reguladoras de Ácido Ribonucleico/genética
Sequências Reguladoras de Ácido Ribonucleico/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, rev); 0 (RNA, Messenger); 0 (RNA, Viral); 0 (Regulatory Sequences, Ribonucleic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170921
[Lr] Data última revisão:
170921
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E16-08-0612


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[PMID]:27411804
[Au] Autor:Ma J; Zhang Z; Yao Q; Su C; Yin X; Wang X
[Ad] Endereço:1​ State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150001, PR China.
[Ti] Título:Regulation of Rev expression by the equine infectious anaemia virus tat-rev mRNA Kozak sequence and its potential influence on viral replication.
[So] Source:J Gen Virol;97(9):2421-6, 2016 Sep.
[Is] ISSN:1465-2099
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Rev, an important accessory protein of equine infectious anaemia virus (EIAV), induces the nuclear export of incompletely spliced viral mRNAs. Rev is translated from the tat-rev mRNA through leaky scanning of the tat CUG. In this study, the function of the Kozak sequence at the beginning of the rev ORF was investigated. Deletion or attenuation of the Kozak sequence resulted in expression of an N-terminal 11 aa-truncated Rev in addition to WT Rev. Truncated Rev displayed weaker promotion of Gag expression and processing than WT Rev. Furthermore, EIAV rescued from an infectious molecular clone (pEIAVUK3) with Kozak attenuation exhibited decreased viral replication in host cells in vitro. These results provide a new understanding of the relationship between EIAV Rev expression and viral replication.
[Mh] Termos MeSH primário: Regulação Viral da Expressão Gênica
Produtos do Gene rev/biossíntese
Produtos do Gene tat/biossíntese
Vírus da Anemia Infecciosa Equina/genética
Biossíntese de Proteínas
RNA Mensageiro/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: Linhagem Celular
Produtos do Gene rev/genética
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, rev); 0 (Gene Products, tat); 0 (RNA, Messenger)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170501
[Lr] Data última revisão:
170501
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160715
[St] Status:MEDLINE
[do] DOI:10.1099/jgv.0.000548


  3 / 947 MEDLINE  
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[PMID]:26059226
[Au] Autor:Lata S; Ali A; Sood V; Raja R; Banerjea AC
[Ad] Endereço:Department of Microbiology, University College of Medical Sciences and Guru Teg Bahadur Hospital, Delhi 110095, India.
[Ti] Título:HIV-1 Rev downregulates Tat expression and viral replication via modulation of NAD(P)H:quinine oxidoreductase 1 (NQO1).
[So] Source:Nat Commun;6:7244, 2015 Jun 10.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: HIV-1 gene expression and replication largely depend on the regulatory proteins Tat and Rev, but it is unclear how the intracellular levels of these viral proteins are regulated after infection. Here we report that HIV-1 Rev causes specific degradation of cytoplasmic Tat, which results in inhibition of HIV-1 replication. The nuclear export signal (NES) region of Rev is crucial for this activity but is not involved in direct interactions with Tat. Rev reduces the levels of ubiquitinated forms of Tat, which have previously been reported to be important for its transcriptional properties. Tat is stabilized in the presence of NAD(P)H: quinine oxidoreductase 1 (NQO1), and potent degradation of Tat is induced by dicoumarol, an NQO1 inhibitor. Furthermore, Rev causes specific reduction in the levels of endogenous NQO1. Thus, we propose that Rev is able to induce degradation of Tat indirectly by downregulating NQO1 levels. Our findings have implications in HIV-1 gene expression and latency.
[Mh] Termos MeSH primário: Produtos do Gene rev/metabolismo
Produtos do Gene tat/metabolismo
HIV-1/metabolismo
NAD(P)H Desidrogenase (Quinona)/metabolismo
Replicação Viral
[Mh] Termos MeSH secundário: HIV-1/fisiologia
Sinais de Exportação Nuclear
Proteólise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Gene Products, rev); 0 (Gene Products, tat); 0 (Nuclear Export Signals); EC 1.6.5.2 (NAD(P)H Dehydrogenase (Quinone)); EC 1.6.5.2 (NQO1 protein, human)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150611
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms8244


  4 / 947 MEDLINE  
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[PMID]:26058812
[Au] Autor:Nam D; Chatterjee S; Yin H; Liu R; Lee J; Yechoor VK; Ma K
[Ad] Endereço:Center for Diabetes Research, Department of Medicine, Houston Methodist Research Institute, Houston, TX, 77030.
[Ti] Título:Novel Function of Rev-erbα in Promoting Brown Adipogenesis.
[So] Source:Sci Rep;5:11239, 2015 Jun 10.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Brown adipose tissue is a major thermogenic organ that plays a key role in maintenance of body temperature and whole-body energy homeostasis. Rev-erbα, a ligand-dependent nuclear receptor and transcription repressor of the molecular clock, has been implicated in the regulation of adipogenesis. However, whether Rev-erbα participates in brown fat formation is not known. Here we show that Rev-erbα is a key regulator of brown adipose tissue development by promoting brown adipogenesis. Genetic ablation of Rev-erbα in mice severely impairs embryonic and neonatal brown fat formation accompanied by loss of brown identity. This defect is due to a cell-autonomous function of Rev-erbα in brown adipocyte lineage commitment and terminal differentiation, as demonstrated by genetic loss- and gain-of-function studies in mesenchymal precursors and brown preadipocytes. Moreover, pharmacological activation of Rev-erbα activity promotes, whereas its inhibition suppresses brown adipocyte differentiation. Mechanistic investigations reveal that Rev-erbα represses key components of the TGF-ß cascade, an inhibitory pathway of brown fat development. Collectively, our findings delineate a novel role of Rev-erbα in driving brown adipocyte development, and provide experimental evidence that pharmacological interventions of Rev-erbα may offer new avenues for the treatment of obesity and related metabolic disorders.
[Mh] Termos MeSH primário: Tecido Adiposo Marrom/crescimento & desenvolvimento
Produtos do Gene rev/fisiologia
[Mh] Termos MeSH secundário: Tecido Adiposo Marrom/citologia
Animais
Diferenciação Celular
Camundongos
Camundongos Endogâmicos C57BL
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Gene Products, rev)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150611
[St] Status:MEDLINE
[do] DOI:10.1038/srep11239


  5 / 947 MEDLINE  
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[PMID]:25798852
[Au] Autor:Kang JI; Park CI; Namkoong K; Kim SJ
[Ad] Endereço:Department of Psychiatry and.
[Ti] Título:Associations between polymorphisms in the NR1D1 gene encoding for nuclear receptor REV-ERBα and circadian typologies.
[So] Source:Chronobiol Int;32(4):568-72, 2015 May.
[Is] ISSN:1525-6073
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nuclear receptor REV-ERBα, a key component of an internal timekeeping system, has been considered to be related to disrupted circadian rhythms and mood disorder. In this study, we aimed to evaluate the relationship between the genotype frequencies of single gene polymorphisms (SNPs) of the NR1D1 gene encoding REV-ERBα and circadian typologies. The classification of chronotypes and genotyping of three SNPs (rs2314339, rs2071427, rs12941497) of the NR1D1 gene were conducted in 602 healthy young adults (355 males, 247 females). A significant association was found between the genotypes of rs12941497 and three chronotype categories. These findings support the role of NR1D1 polymorphisms in the regulation of circadian rhythms.
[Mh] Termos MeSH primário: Ritmo Circadiano/genética
Produtos do Gene rev/genética
Genótipo
Transtornos do Humor/genética
Membro 1 do Grupo D da Subfamília 1 de Receptores Nucleares/genética
Polimorfismo de Nucleotídeo Único/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Feminino
Seres Humanos
Masculino
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Gene Products, rev); 0 (NR1D1 protein, human); 0 (Nuclear Receptor Subfamily 1, Group D, Member 1)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150505
[Lr] Data última revisão:
150505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150324
[St] Status:MEDLINE
[do] DOI:10.3109/07420528.2015.1006327


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[PMID]:25723178
[Au] Autor:Mahboobi SH; Javanpour AA; Mofrad MR
[Ad] Endereço:Molecular Cell Biomechanics Laboratory, Departments of Bioengineering and Mechanical Engineering, University of California, Berkeley, California, United States of America.
[Ti] Título:The interaction of RNA helicase DDX3 with HIV-1 Rev-CRM1-RanGTP complex during the HIV replication cycle.
[So] Source:PLoS One;10(2):e0112969, 2015.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Molecular traffic between the nucleus and the cytoplasm is regulated by the nuclear pore complex (NPC), which acts as a highly selective channel perforating the nuclear envelope in eukaryotic cells. The human immunodeficiency virus (HIV) exploits the nucleocytoplasmic pathway to export its RNA transcripts across the NPC to the cytoplasm. Despite extensive study on the HIV life cycle and the many drugs developed to target this cycle, no current drugs have been successful in targeting the critical process of viral nuclear export, even though HIV's reliance on a single host protein, CRM1, to export its unspliced and partially spliced RNA transcripts makes it a tempting target. Due to recent findings implicating a DEAD-box helicase, DDX3, in HIV replication and a member of the export complex, it has become an appealing target for anti-HIV drug inhibition. In the present research, we have applied a hybrid computational protocol to analyze protein-protein interactions in the HIV mRNA export cycle. This method is based on molecular docking followed by molecular dynamics simulation and accompanied by approximate free energy calculation (MM/GBSA), computational alanine scanning, clustering, and evolutionary analysis. We highlight here some of the most likely binding modes and interfacial residues between DDX3 and CRM1 both in the absence and presence of RanGTP. This work shows that although DDX3 can bind to free CRM1, addition of RanGTP leads to more concentrated distribution of binding modes and stronger binding between CRM1 and RanGTP.
[Mh] Termos MeSH primário: RNA Helicases DEAD-box/metabolismo
Produtos do Gene rev/metabolismo
Infecções por HIV/metabolismo
HIV-1
Carioferinas/metabolismo
Receptores Citoplasmáticos e Nucleares/metabolismo
Replicação Viral
Proteína ran de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
RNA Helicases DEAD-box/química
Produtos do Gene rev/química
Infecções por HIV/virologia
HIV-1/fisiologia
Seres Humanos
Carioferinas/química
Modelos Moleculares
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
Complexos Multiproteicos/química
Complexos Multiproteicos/metabolismo
Ligação Proteica
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Receptores Citoplasmáticos e Nucleares/química
Relação Estrutura-Atividade
Proteína ran de Ligação ao GTP/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Gene Products, rev); 0 (Karyopherins); 0 (Multiprotein Complexes); 0 (Receptors, Cytoplasmic and Nuclear); 0 (exportin 1 protein); EC 3.6.1.- (DDX3X protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases); EC 3.6.5.2 (ran GTP-Binding Protein)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:150305
[Lr] Data última revisão:
150305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0112969


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[PMID]:25503645
[Au] Autor:Zhong F; Geng G; Chen B; Pan T; Li Q; Zhang H; Bai C
[Ad] Endereço:Institute of Human Virology, Key Laboratory of Tropical Diseases Control of Ministry of Education of China, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, 510080, China. zhangh92@mail.sysu.edu.cn baichuan@mail.sysu.edu.cn.
[Ti] Título:Identification of benzenesulfonamide quinoline derivatives as potent HIV-1 replication inhibitors targeting Rev protein.
[So] Source:Org Biomol Chem;13(6):1792-9, 2015 Feb 14.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human immunodeficiency virus type 1 (HIV-1) Rev protein facilitates the export of viral RNA from nucleus to cytoplasm, which is a key step in HIV-1 pathogenesis and transmission. In this study, we have screened a commercial library and identified the hit compound 1 bearing a benzenesulfonamide quinoline scaffold that inhibited Rev activity and HIV-1 infectivity. Compounds bearing this scaffold were synthesized and their SAR was studied. We identified compound 20 with low toxicity and potent activity to inhibit HIV-1 replication by affecting Rev function.
[Mh] Termos MeSH primário: Fármacos Anti-HIV/farmacologia
Derivados de Benzeno/farmacologia
Produtos do Gene rev/antagonistas & inibidores
HIV-1/efeitos dos fármacos
Quinolinas/farmacologia
Sulfonamidas/farmacologia
Replicação Viral/efeitos dos fármacos
[Mh] Termos MeSH secundário: Fármacos Anti-HIV/síntese química
Fármacos Anti-HIV/química
Derivados de Benzeno/síntese química
Derivados de Benzeno/química
Produtos do Gene rev/metabolismo
HIV-1/crescimento & desenvolvimento
HIV-1/metabolismo
Estrutura Molecular
Quinolinas/síntese química
Quinolinas/química
Sulfonamidas/síntese química
Sulfonamidas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-HIV Agents); 0 (Benzene Derivatives); 0 (Gene Products, rev); 0 (Quinolines); 0 (Sulfonamides)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:150128
[Lr] Data última revisão:
150128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141216
[St] Status:MEDLINE
[do] DOI:10.1039/c4ob02247e


  8 / 947 MEDLINE  
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[PMID]:25533001
[Au] Autor:Umunnakwe CN; Loyd H; Cornick K; Chavez JR; Dobbs D; Carpenter S
[Ad] Endereço:Department of Animal Science, Iowa State University, Ames, IA, 50011, USA. nkemjika@iastate.edu.
[Ti] Título:Computational modeling suggests dimerization of equine infectious anemia virus Rev is required for RNA binding.
[So] Source:Retrovirology;11:115, 2014 Dec 23.
[Is] ISSN:1742-4690
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The lentiviral Rev protein mediates nuclear export of intron-containing viral RNAs that encode structural proteins or serve as the viral genome. Following translation, HIV-1 Rev localizes to the nucleus and binds its cognate sequence, termed the Rev-responsive element (RRE), in incompletely spliced viral RNA. Rev subsequently multimerizes along the viral RNA and associates with the cellular Crm1 export machinery to translocate the RNA-protein complex to the cytoplasm. Equine infectious anemia virus (EIAV) Rev is functionally homologous to HIV-1 Rev, but shares very little sequence similarity and differs in domain organization. EIAV Rev also contains a bipartite RNA binding domain comprising two short arginine-rich motifs (designated ARM-1 and ARM-2) spaced 79 residues apart in the amino acid sequence. To gain insight into the topology of the bipartite RNA binding domain, a computational approach was used to model the tertiary structure of EIAV Rev. RESULTS: The tertiary structure of EIAV Rev was modeled using several protein structure prediction and model quality assessment servers. Two types of structures were predicted: an elongated structure with an extended central alpha helix, and a globular structure with a central bundle of helices. Assessment of models on the basis of biophysical properties indicated they were of average quality. In almost all models, ARM-1 and ARM-2 were spatially separated by >15 Å, suggesting that they do not form a single RNA binding interface on the monomer. A highly conserved canonical coiled-coil motif was identified in the central region of EIAV Rev, suggesting that an RNA binding interface could be formed through dimerization of Rev and juxtaposition of ARM-1 and ARM-2. In support of this, purified Rev protein migrated as a dimer in Blue native gels, and mutation of a residue predicted to form a key coiled-coil contact disrupted dimerization and abrogated RNA binding. In contrast, mutation of residues outside the predicted coiled-coil interface had no effect on dimerization or RNA binding. CONCLUSIONS: Our results suggest that EIAV Rev binding to the RRE requires dimerization via a coiled-coil motif to juxtapose two RNA binding motifs, ARM-1 and ARM-2.
[Mh] Termos MeSH primário: Produtos do Gene rev/química
Produtos do Gene rev/metabolismo
Vírus da Anemia Infecciosa Equina/fisiologia
Multimerização Proteica
RNA Viral/metabolismo
[Mh] Termos MeSH secundário: Modelos Moleculares
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Gene Products, rev); 0 (RNA, Viral)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141224
[St] Status:MEDLINE
[do] DOI:10.1186/s12977-014-0115-7


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[PMID]:24515490
[Au] Autor:Stahl SJ; Watts NR; Wingfield PT
[Ad] Endereço:Protein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD, USA.
[Ti] Título:Generation and use of antibody fragments for structural studies of proteins refractory to crystallization.
[So] Source:Methods Mol Biol;1131:549-61, 2014.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:With the rapid technological advances in all aspects of macromolecular X-ray crystallography the preparation of diffraction quality crystals has become the rate-limiting step. Crystallization chaperones have proven effective for overcoming this barrier. Here we describe the usage of a Fab chaperone for the crystallization of HIV-1 Rev, a protein that has long resisted all attempts at elucidating its complete atomic structure.
[Mh] Termos MeSH primário: Biotecnologia/métodos
Cristalografia por Raios X
Produtos do Gene rev/metabolismo
HIV-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (Gene Products, rev)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140212
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-62703-992-5_35


  10 / 947 MEDLINE  
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[PMID]:24478440
[Au] Autor:Sakuma T; Davila JI; Malcolm JA; Kocher JP; Tonne JM; Ikeda Y
[Ad] Endereço:Department of Molecular Medicine, Mayo Clinic, Rochester, Minnesota, USA.
[Ti] Título:Murine leukemia virus uses NXF1 for nuclear export of spliced and unspliced viral transcripts.
[So] Source:J Virol;88(8):4069-82, 2014 Apr.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:UNLABELLED: Intron-containing mRNAs are subject to restricted nuclear export in higher eukaryotes. Retroviral replication requires the nucleocytoplasmic transport of both spliced and unspliced RNA transcripts, and RNA export mechanisms of gammaretroviruses are poorly characterized. Here, we report the involvement of the nuclear export receptor NXF1/TAP in the nuclear export of gammaretroviral RNA transcripts. We identified a conserved cis-acting element in the pol gene of gammaretroviruses, including murine leukemia virus (MLV) and xenotropic murine leukemia virus (XMRV), named the CAE (cytoplasmic accumulation element). The CAE enhanced the cytoplasmic accumulation of viral RNA transcripts and the expression of viral proteins without significantly affecting the stability, splicing, or translation efficiency of the transcripts. Insertion of the CAE sequence also facilitated Rev-independent HIV Gag expression. We found that the CAE sequence interacted with NXF1, whereas disruption of NXF1 ablated CAE function. Thus, the CAE sequence mediates the cytoplasmic accumulation of gammaretroviral transcripts in an NXF1-dependent manner. Disruption of NXF1 expression impaired cytoplasmic accumulations of both spliced and unspliced RNA transcripts of XMRV and MLV, resulting in their nuclear retention or degradation. Thus, our results demonstrate that gammaretroviruses use NXF1 for the cytoplasmic accumulation of both spliced and nonspliced viral RNA transcripts. IMPORTANCE: Murine leukemia virus (MLV) has been studied as one of the classic models of retrovirology. Although unspliced host messenger RNAs are rarely exported from the nucleus, MLV actively exports unspliced viral RNAs to the cytoplasm. Despite extensive studies, how MLV achieves this difficult task has remained a mystery. Here, we have studied the RNA export mechanism of MLV and found that (i) the genome contains a sequence which supports the efficient nuclear export of viral RNAs, (ii) the cellular factor NXF1 is involved in the nuclear export of both spliced and unspliced viral RNAs, and, finally, (iii) depletion of NXF1 results in nuclear retention or degradation of viral RNAs. Our study provides a novel insight into MLV nuclear export.
[Mh] Termos MeSH primário: Vírus da Leucemia Murina/metabolismo
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Processamento de RNA
RNA Viral/metabolismo
Infecções por Retroviridae/veterinária
Doenças dos Roedores/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Animais
Sequência de Bases
Linhagem Celular
Núcleo Celular/genética
Núcleo Celular/metabolismo
Núcleo Celular/virologia
Produtos do Gene rev/genética
Produtos do Gene rev/metabolismo
Vírus da Leucemia Murina/genética
Camundongos
Dados de Sequência Molecular
Proteínas de Transporte Nucleocitoplasmático/genética
RNA Viral/genética
Infecções por Retroviridae/genética
Infecções por Retroviridae/metabolismo
Infecções por Retroviridae/virologia
Doenças dos Roedores/genética
Doenças dos Roedores/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Gene Products, rev); 0 (NXF1 protein, mouse); 0 (Nucleocytoplasmic Transport Proteins); 0 (RNA, Viral)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140131
[St] Status:MEDLINE
[do] DOI:10.1128/JVI.03584-13



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