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[PMID]:29221753
[Au] Autor:Daniel DC; Johnson EM
[Ad] Endereço:Department of Microbiology and Molecular Cell Biology, Eastern Virginia Medical School, Norfolk, VA 23507, USA.
[Ti] Título:PURA, the gene encoding Pur-alpha, member of an ancient nucleic acid-binding protein family with mammalian neurological functions.
[So] Source:Gene;643:133-143, 2018 Feb 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The PURA gene encodes Pur-alpha, a 322 amino acid protein with repeated nucleic acid binding domains that are highly conserved from bacteria through humans. PUR genes with a single copy of this domain have been detected so far in spirochetes and bacteroides. Lower eukaryotes possess one copy of the PUR gene, whereas chordates possess 1 to 4 PUR family members. Human PUR genes encode Pur-alpha (Pura), Pur-beta (Purb) and two forms of Pur-gamma (Purg). Pur-alpha is a protein that binds specific DNA and RNA sequence elements. Human PURA, located at chromosome band 5q31, is under complex control of three promoters. The entire protein coding sequence of PURA is contiguous within a single exon. Several studies have found that overexpression or microinjection of Pura inhibits anchorage-independent growth of oncogenically transformed cells and blocks proliferation at either G1-S or G2-M checkpoints. Effects on the cell cycle may be mediated by interaction of Pura with cellular proteins including Cyclin/Cdk complexes and the Rb tumor suppressor protein. PURA knockout mice die shortly after birth with effects on brain and hematopoietic development. In humans environmentally induced heterozygous deletions of PURA have been implicated in forms of myelodysplastic syndrome and progression to acute myelogenous leukemia. Pura plays a role in AIDS through association with the HIV-1 protein, Tat. In the brain Tat and Pura association in glial cells activates transcription and replication of JC polyomavirus, the agent causing the demyelination disease, progressive multifocal leukoencephalopathy. Tat and Pura also act to stimulate replication of the HIV-1 RNA genome. In neurons Pura accompanies mRNA transcripts to sites of translation in dendrites. Microdeletions in the PURA locus have been implicated in several neurological disorders. De novo PURA mutations have been related to a spectrum of phenotypes indicating a potential PURA syndrome. The nucleic acid, G-rich Pura binding element is amplified as expanded polynucleotide repeats in several brain diseases including fragile X syndrome and a familial form of amyotrophic lateral sclerosis/fronto-temporal dementia. Throughout evolution the Pura protein plays a critical role in survival, based on conservation of its nucleic acid binding properties. These Pura properties have been adapted in higher organisms to the as yet unfathomable development of the human brain.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos/genética
Animais
Sequência de Bases
Ciclo Celular
Proteínas de Ciclo Celular/genética
Sequência Conservada/genética
Replicação do DNA
Células Dendríticas/metabolismo
HIV-1/genética
Seres Humanos
Leucemia Mieloide Aguda/genética
Síndromes Mielodisplásicas/genética
Neuroglia/metabolismo
Neurônios/metabolismo
Proteínas com Motivo de Reconhecimento de RNA/genética
Proteínas com Motivo de Reconhecimento de RNA/metabolismo
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (DNA-Binding Proteins); 0 (PURA protein, human); 0 (RNA Recognition Motif Proteins); 0 (RNA, Messenger); 0 (Transcription Factors)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171210
[St] Status:MEDLINE


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[PMID]:28755480
[Au] Autor:Galan A; Lozano G; Piñeiro D; Martinez-Salas E
[Ad] Endereço:Centro de Biologia Molecular Severo Ochoa, Consejo Superior de Investigaciones Cientificas, Universidad Autonoma de Madrid, Spain.
[Ti] Título:G3BP1 interacts directly with the FMDV IRES and negatively regulates translation.
[So] Source:FEBS J;284(19):3202-3217, 2017 Oct.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RNA-protein interactions play a pivotal role in the function of picornavirus internal ribosome entry site (IRES) elements. Here we analysed the impact of Ras GTPase SH3 domain binding protein 1 (G3BP1) in the IRES activity of foot-and-mouth disease virus (FMDV). We found that G3BP1 interacts directly with three distinct sequences of the IRES element using RNA electrophoretic mobility-shift assays. Analysis of the interaction with domain 5 indicated that the G3BP1 binding-site is placed at the single-stranded region although it allows large sequence heterogeneity and the hairpin located upstream of this region enhances retarded complex formation. In addition, G3BP1 interacts directly with the polypyrimidine tract-binding protein and the translation initiation factor 4B (eIF4B) through the C-terminal region. Moreover, G3BP1 is cleaved during FMDV infection yielding two fragments, Ct-G3BP1 and Nt-G3BP1. Both fragments inhibit cap- and IRES-dependent translation, but the Ct-G3BP1 fragment shows a stronger effect on IRES-dependent translation. Assembly of complexes with G3BP1 results in a significantly reduced local flexibility of the IRES element, consistent with the negative effect of this protein. Our results highlight the IRES-binding capacity of G3BP1 and illustrate its function as a translation inhibitor.
[Mh] Termos MeSH primário: Proteínas de Transporte/química
Fatores de Iniciação em Eucariotos/genética
Vírus da Febre Aftosa/química
Sítios Internos de Entrada Ribossomal
Biossíntese de Proteínas
RNA Viral/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Clonagem Molecular
DNA Helicases
Escherichia coli/genética
Escherichia coli/metabolismo
Fatores de Iniciação em Eucariotos/química
Fatores de Iniciação em Eucariotos/metabolismo
Vírus da Febre Aftosa/genética
Vírus da Febre Aftosa/metabolismo
Expressão Gênica
Células HEK293
Seres Humanos
Cinética
Conformação de Ácido Nucleico
Proteínas de Ligação a Poli-ADP-Ribose
Ligação Proteica
RNA Helicases
Proteínas com Motivo de Reconhecimento de RNA
RNA Viral/genética
RNA Viral/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ribossomos/genética
Ribossomos/metabolismo
Técnica de Seleção de Aptâmeros
Alinhamento de Sequência
Homologia de Sequência do Ácido Nucleico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Eukaryotic Initiation Factors); 0 (Internal Ribosome Entry Sites); 0 (Poly-ADP-Ribose Binding Proteins); 0 (RNA Recognition Motif Proteins); 0 (RNA, Viral); 0 (Recombinant Proteins); 0 (eIF-4B); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (G3BP1 protein, human); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170730
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14184


  3 / 151 MEDLINE  
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[PMID]:28488892
[Au] Autor:Wang X; Chang L; Wang H; Su A; Wu Z
[Ad] Endereço:1 Department of Hematology, Affiliated Nanjing Drum Tower Hospital, Medical School, Nanjing University , Nanjing, People's Republic of China .
[Ti] Título:Dcp1a and GW182 Induce Distinct Cellular Aggregates and Have Different Effects on microRNA Pathway.
[So] Source:DNA Cell Biol;36(7):565-570, 2017 Jul.
[Is] ISSN:1557-7430
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:P-bodies are cytoplasmic foci composed of mRNAs and enzymes involved in mRNA degradation. P-bodies have been found to link to RNA interference and RNA decay mediated by microRNAs (miRNAs) and translational repression. Here, we aim to investigate different effects of overexpressed Dcp1a or GW182 on cytoplasmic aggregates formation and influence on miRNA pathway. Small RNAs were recruited into endogenous foci of P-bodies and aggregates formed by Dcpa1 and GW182 overexpression. However, only overexpressed Dcp1a but not GW182 was colocalized with DDX6, another component of P-bodies and suppressed protein translation. In addition, we investigated the relationship between stress granules and miRNA pathway and found that granules induced by G3BP1 overexpression could recruit small RNAs into the granules and repressed protein translation. As Ago2 is a key component of RNA-induced silencing complex, we also investigated the localization of endogenous Ago2 (edo-Ago2) after Dcp1a and GW182 overexpression, and found that endo-Ago2 did not colocalize with the aggregates induced by overexpression of Dcpla, GW182, and G3BP1. Notably, the ability of miRNA to regulate its target was enhanced by the granules induced by Dcp1a and G3BP1 expression. Our results suggest that overexpressed Dcp1a and GW182 can form different cytoplasmic aggregates and play distinct biological roles in the miRNA pathway.
[Mh] Termos MeSH primário: Autoantígenos/genética
Proteínas de Transporte/genética
Endorribonucleases/genética
MicroRNAs/genética
Interferência de RNA
Proteínas de Ligação a RNA/genética
Transativadores/genética
[Mh] Termos MeSH secundário: Proteínas Argonauta/genética
Proteínas Argonauta/metabolismo
Autoantígenos/metabolismo
Proteínas de Transporte/metabolismo
RNA Helicases DEAD-box/genética
RNA Helicases DEAD-box/metabolismo
DNA Helicases
Endorribonucleases/metabolismo
Células HEK293
Células HeLa
Seres Humanos
Substâncias Macromoleculares/química
Substâncias Macromoleculares/metabolismo
MicroRNAs/metabolismo
Proteínas de Ligação a Poli-ADP-Ribose
Ligação Proteica
Biossíntese de Proteínas
Proteínas Proto-Oncogênicas/genética
Proteínas Proto-Oncogênicas/metabolismo
RNA Helicases
Proteínas com Motivo de Reconhecimento de RNA
Estabilidade de RNA
Proteínas de Ligação a RNA/metabolismo
Transdução de Sinais
Transativadores/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Argonaute Proteins); 0 (Autoantigens); 0 (Carrier Proteins); 0 (EIF2C2 protein, human); 0 (Macromolecular Substances); 0 (MicroRNAs); 0 (Poly-ADP-Ribose Binding Proteins); 0 (Proto-Oncogene Proteins); 0 (RNA Recognition Motif Proteins); 0 (RNA-Binding Proteins); 0 (Trans-Activators); 0 (autoantigen GW182, human); EC 3.1.- (Endoribonucleases); EC 3.1.27.- (DCP1A protein, human); EC 3.6.1.- (DDX6 protein, human); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (G3BP1 protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170511
[St] Status:MEDLINE
[do] DOI:10.1089/dna.2017.3633


  4 / 151 MEDLINE  
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[PMID]:28394340
[Au] Autor:Lu W; Cheng F; Yan W; Li X; Yao X; Song W; Liu M; Shen X; Jiang H; Chen J; Li J; Huang J
[Ad] Endereço:Shanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai, China.
[Ti] Título:Selective targeting p53 lung cancer cells harboring homozygous p53 Arg72 by an inhibitor of CypA.
[So] Source:Oncogene;36(33):4719-4731, 2017 Aug 17.
[Is] ISSN:1476-5594
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:TP53 plays essential roles in tumor initiation and progression, and is frequently mutated in cancer. However, pharmacological stabilization and reactivation of p53 have not been actively explored for targeted cancer therapies. Herein, we identify a novel Cyclophilin A (CypA) small molecule inhibitor (HL001) that induces non-small cell lung cancer (NSCLC) cell cycle arrest and apoptosis via restoring p53 expression. We find that HL001 stabilizes p53 through inhibiting the MDM2-mediated p53 ubiquitination. Further mechanistic studies reveal that the downregulation of G3BP1 and the induction of reactive oxygen species and DNA damage by HL001 contribute to p53 stabilization. Surprisingly, HL001 selectively suppresses tumor growth in p53 wild-type NSCLC harboring Arg72 homozygous alleles (p53-72R) through disrupting interaction between MDM2 and p53-72R in a CypA-dependent manner. Moreover, combining HL001 with cisplatin synergistically enhance tumor regression in orthotopic NSCLC mouse model. Collectively, this study demonstrates that pharmacologic inhibition of CypA offers a potential therapeutic strategy via specific activation of p53-72R in NSCLC.
[Mh] Termos MeSH primário: Antineoplásicos/uso terapêutico
Carcinoma Pulmonar de Células não Pequenas/tratamento farmacológico
Ciclofilina A/antagonistas & inibidores
Inibidores Enzimáticos/uso terapêutico
Fluorenos/uso terapêutico
Neoplasias Pulmonares/tratamento farmacológico
Terapia de Alvo Molecular
Proteína Supressora de Tumor p53/metabolismo
Ureia/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/química
Antineoplásicos/farmacologia
Apoptose/efeitos dos fármacos
Carcinoma Pulmonar de Células não Pequenas/genética
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Pontos de Checagem do Ciclo Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Cisplatino/uso terapêutico
DNA Helicases
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Fluorenos/química
Fluorenos/farmacologia
Homozigoto
Seres Humanos
Estimativa de Kaplan-Meier
Neoplasias Pulmonares/genética
Camundongos
Camundongos Nus
Proteínas de Ligação a Poli-ADP-Ribose
Estabilidade Proteica/efeitos dos fármacos
Proteólise/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-mdm2/metabolismo
RNA Helicases
Proteínas com Motivo de Reconhecimento de RNA
Proteína Supressora de Tumor p53/genética
Ureia/química
Ureia/farmacologia
Ureia/uso terapêutico
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Carrier Proteins); 0 (Enzyme Inhibitors); 0 (Fluorenes); 0 (HL001 compound); 0 (Poly-ADP-Ribose Binding Proteins); 0 (RNA Recognition Motif Proteins); 0 (Tumor Suppressor Protein p53); 8W8T17847W (Urea); EC 2.3.2.27 (Proto-Oncogene Proteins c-mdm2); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (G3BP1 protein, human); EC 3.6.4.13 (RNA Helicases); EC 5.2.1.- (Cyclophilin A); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE
[do] DOI:10.1038/onc.2017.41


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[PMID]:28306503
[Au] Autor:Boeynaems S; Bogaert E; Kovacs D; Konijnenberg A; Timmerman E; Volkov A; Guharoy M; De Decker M; Jaspers T; Ryan VH; Janke AM; Baatsen P; Vercruysse T; Kolaitis RM; Daelemans D; Taylor JP; Kedersha N; Anderson P; Impens F; Sobott F; Schymkowitz J; Rousseau F; Fawzi NL; Robberecht W; Van Damme P; Tompa P; Van Den Bosch L
[Ad] Endereço:Experimental Neurology and Leuven Research Institute for Neuroscience and Disease (LIND), Department of Neurosciences, KU Leuven - University of Leuven, 3000 Leuven, Belgium; Laboratory of Neurobiology, VIB, Center for Brain and Disease Research, 3000 Leuven, Belgium.
[Ti] Título:Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics.
[So] Source:Mol Cell;65(6):1044-1055.e5, 2017 Mar 16.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Liquid-liquid phase separation (LLPS) of RNA-binding proteins plays an important role in the formation of multiple membrane-less organelles involved in RNA metabolism, including stress granules. Defects in stress granule homeostasis constitute a cornerstone of ALS/FTLD pathogenesis. Polar residues (tyrosine and glutamine) have been previously demonstrated to be critical for phase separation of ALS-linked stress granule proteins. We now identify an active role for arginine-rich domains in these phase separations. Moreover, arginine-rich dipeptide repeats (DPRs) derived from C9orf72 hexanucleotide repeat expansions similarly undergo LLPS and induce phase separation of a large set of proteins involved in RNA and stress granule metabolism. Expression of arginine-rich DPRs in cells induced spontaneous stress granule assembly that required both eIF2α phosphorylation and G3BP. Together with recent reports showing that DPRs affect nucleocytoplasmic transport, our results point to an important role for arginine-rich DPRs in the pathogenesis of C9orf72 ALS/FTLD.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/metabolismo
Arginina/metabolismo
Grânulos Citoplasmáticos/metabolismo
Dipeptídeos/metabolismo
Proteínas Intrinsicamente Desordenadas/metabolismo
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Esclerose Amiotrófica Lateral/genética
Esclerose Amiotrófica Lateral/patologia
Arginina/química
Proteína C9orf72
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Grânulos Citoplasmáticos/patologia
DNA Helicases
Dipeptídeos/química
Fator de Iniciação 2 em Eucariotos/genética
Fator de Iniciação 2 em Eucariotos/metabolismo
Células HeLa
Seres Humanos
Proteínas Intrinsicamente Desordenadas/química
Gotículas Lipídicas/metabolismo
Fosforilação
Proteínas de Ligação a Poli-ADP-Ribose
Domínios Proteicos
Proteínas/química
RNA/metabolismo
RNA Helicases
Proteínas com Motivo de Reconhecimento de RNA
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (C9orf72 Protein); 0 (C9orf72 protein, human); 0 (Carrier Proteins); 0 (Dipeptides); 0 (Eukaryotic Initiation Factor-2); 0 (Intrinsically Disordered Proteins); 0 (Poly-ADP-Ribose Binding Proteins); 0 (Proteins); 0 (RNA Recognition Motif Proteins); 63231-63-0 (RNA); 94ZLA3W45F (Arginine); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (G3BP1 protein, human); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE


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[PMID]:28213559
[Au] Autor:Hackett JB; Shi X; Kobylarz AT; Lucas MK; Wessendorf RL; Hines KM; Bentolila S; Hanson MR; Lu Y
[Ad] Endereço:Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410 (J.B.H., A.T.K., M.K.L., R.L.W., Y.L.); and.
[Ti] Título:An Organelle RNA Recognition Motif Protein Is Required for Photosystem II Subunit Transcript Editing.
[So] Source:Plant Physiol;173(4):2278-2293, 2017 Apr.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Loss-of-function mutations in ORGANELLE RNA RECOGNITION MOTIF PROTEIN6 (ORRM6) result in the near absence of RNA editing of -C77 and the reduction in -C794 editing in Arabidopsis ( ). The mutants have decreased levels of photosystem II (PSII) proteins, especially PsbF, lower PSII activity, pale green pigmentation, smaller leaf and plant sizes, and retarded growth. Stable expression of rescues the editing defects and mutant phenotype. Unlike ORRM1, the other known ORRM plastid editing factor, ORRM6, does not contain RNA editing interacting protein/multiple organellar RNA editing factor (RIP/MORF) boxes, which are required for ORRM1 to interact with site-specific pentatricopeptide repeat protein editing factors. ORRM6 interacts with RIP1/MORF8, RIP2/MORF2, and RIP9/MORF9, known components of RNA editosomes. While some plastid RRM proteins are involved in other forms of RNA processing and translation, the primary function of ORRM6 is evidently to mediate -C77 editing, like the essential site-specific pentatricopeptide repeat protein LOW PSII ACCUMULATION66. Stable expression in the mutants of a nucleus-encoded, plastid-targeted PsbF protein from a gene carrying a T at nucleotide 77 significantly increases leaf and plant sizes, chlorophyll content, and PSII activity. These transformants demonstrate that plastid RNA editing can be bypassed through the expression of nucleus-encoded, edited forms of plastid genes.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Grupo dos Citocromos b/metabolismo
Organelas/metabolismo
Complexo de Proteína do Fotossistema II/metabolismo
Edição de RNA
Proteínas com Motivo de Reconhecimento de RNA/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Núcleo Celular/genética
Núcleo Celular/metabolismo
Clorofila/metabolismo
Grupo dos Citocromos b/genética
Regulação da Expressão Gênica de Plantas
Immunoblotting
Mutação
Organelas/genética
Fenótipo
Fotossíntese/genética
Complexo de Proteína do Fotossistema II/genética
Plantas Geneticamente Modificadas
Plastídeos/genética
Plastídeos/metabolismo
Ligação Proteica
Proteínas com Motivo de Reconhecimento de RNA/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cytochrome b Group); 0 (ORRM6 protein, Arabidopsis); 0 (Photosystem II Protein Complex); 0 (RNA Recognition Motif Proteins); 1406-65-1 (Chlorophyll)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170219
[St] Status:MEDLINE
[do] DOI:10.1104/pp.16.01623


  7 / 151 MEDLINE  
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[PMID]:28201607
[Au] Autor:Haag S; Schindler M; Berndt L; Brennicke A; Takenaka M; Weber G
[Ad] Endereço:Molekulare Botanik, Universität Ulm, 89069 Ulm, Germany.
[Ti] Título:Crystal structures of the Arabidopsis thaliana organellar RNA editing factors MORF1 and MORF9.
[So] Source:Nucleic Acids Res;45(8):4915-4928, 2017 May 05.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In flowering plant plastids and mitochondria, multiple organellar RNA editing factor (MORF/RIP) proteins are required at most sites for efficient C to U RNA editing catalyzed by the RNA editosome. MORF proteins harbor a conserved stretch of residues (MORF-box), form homo- and heteromers and interact with selected PPR (pentatricopeptide repeat) proteins, which recognize each editing site. The molecular function of the MORF-box remains elusive since it shares no sequence similarity with known domains. We determined structures of the A. thaliana mitochondrial MORF1 and chloroplast MORF9 MORF-boxes which both adopt a novel globular fold (MORF domain). Our structures state a paradigmatic model for MORF domains and their specific dimerization via a hydrophobic interface. We cross-validate the interface by yeast two-hybrid studies and pulldown assays employing structure-based mutants. We find a structural similarity of the MORF domain to an N-terminal ferredoxin-like domain (NFLD), which confers RNA substrate positioning in bacterial 4-thio-uracil tRNA synthetases, implying direct RNA contacts of MORF proteins during RNA editing. With the MORF1 and MORF9 structures we elucidate a yet unknown fold, corroborate MORF interaction studies, validate the mechanism of MORF multimerization by structure-based mutants and pave the way towards a complete structural characterization of the plant RNA editosome.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/química
Arabidopsis/química
Domínios Proteicos/genética
Proteínas com Motivo de Reconhecimento de RNA/química
Proteínas de Ligação a RNA/química
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Cloroplastos/química
Cristalografia por Raios X
Mitocôndrias/química
Dados de Sequência Molecular
Dobramento de Proteína
Estrutura Terciária de Proteína
Edição de RNA/genética
Proteínas com Motivo de Reconhecimento de RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (MORF1 protein, Arabidopsis); 0 (MORF9 protein, Arabidopsis); 0 (RNA Recognition Motif Proteins); 0 (RNA-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170216
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx099


  8 / 151 MEDLINE  
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[PMID]:28079881
[Au] Autor:Lai CH; Huang YC; Lee JC; Tseng JT; Chang KC; Chen YJ; Ding NJ; Huang PH; Chang WC; Lin BW; Chen RY; Wang YC; Lai YC; Hung LY
[Ad] Endereço:Institute of Bioinformatics and Biosignal Transduction, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan 70101, Taiwan.
[Ti] Título:Translational upregulation of Aurora-A by hnRNP Q1 contributes to cell proliferation and tumorigenesis in colorectal cancer.
[So] Source:Cell Death Dis;8(1):e2555, 2017 Jan 12.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:By using RNA-immunoprecipitation assay following next-generation sequencing, a group of cell cycle-related genes targeted by hnRNP Q1 were identified, including Aurora-A kinase. Overexpressed hnRNP Q1 can upregulate Aurora-A protein, but not alter the mRNA level, through enhancing the translational efficiency of Aurora-A mRNA, either in a cap-dependent or -independent manner, by interacting with the 5'-UTR of Aurora-A mRNA through its RNA-binding domains (RBDs) 2 and 3. By ribosomal profiling assay further confirmed the translational regulation of Aurora-A mRNA by hnRNP Q1. Overexpression of hnRNP Q1 promotes cell proliferation and tumor growth. HnRNP Q1/ΔRBD23-truncated mutant, which loses the binding ability and translational regulation of Aurora-A mRNA, has no effect on promoting tumor growth. The expression level of hnRNP Q1 is positively correlated with Aurora-A in colorectal cancer. Taken together, our data indicate that hnRNP Q1 is a novel trans-acting factor that binds to Aurora-A mRNA 5'-UTRs and regulates its translation, which increases cell proliferation and contributes to tumorigenesis in colorectal cancer.
[Mh] Termos MeSH primário: Aurora Quinase A/genética
Carcinogênese/genética
Neoplasias Colorretais/genética
Ribonucleoproteínas Nucleares Heterogêneas/genética
[Mh] Termos MeSH secundário: Aurora Quinase A/metabolismo
Linhagem Celular Tumoral
Proliferação Celular/genética
Neoplasias Colorretais/patologia
Feminino
Regulação Neoplásica da Expressão Gênica
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Seres Humanos
Masculino
Proteínas com Motivo de Reconhecimento de RNA
RNA Mensageiro/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (RNA Recognition Motif Proteins); 0 (RNA, Messenger); EC 2.7.11.1 (Aurora Kinase A)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170113
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2016.479


  9 / 151 MEDLINE  
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[PMID]:28013103
[Au] Autor:Le Sage V; Cinti A; McCarthy S; Amorim R; Rao S; Daino GL; Tramontano E; Branch DR; Mouland AJ
[Ad] Endereço:HIV-1 RNA Trafficking Laboratory, Lady Davis Institute at the Jewish General Hospital, Montréal, Québec, Canada H3T 1E2.
[Ti] Título:Ebola virus VP35 blocks stress granule assembly.
[So] Source:Virology;502:73-83, 2017 Feb.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stress granules (SGs) are dynamic cytoplasmic aggregates of translationally silenced mRNAs that assemble in response to environmental stress. SGs appear to play an important role in antiviral innate immunity and many viruses have evolved to block or subvert SGs components for their own benefit. Here, we demonstrate that intracellular Ebola virus (EBOV) replication and transcription-competent virus like particles (trVLP) infection does not lead to SG assembly but leads to a blockade to Arsenite-induced SG assembly. Moreover we show that EBOV VP35 represses the assembly of canonical and non-canonical SGs induced by a variety of pharmacological stresses. This SG blockade requires, at least in part, the C-terminal domain of VP35. Furthermore, results from our co-immunoprecipitation studies indicate that VP35 interacts with multiple SG components, including G3BP1, eIF3 and eEF2 through a stress- and RNA-independent mechanism. These data suggest a novel function for EBOV VP35 in the repression of SG assembly.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/virologia
Ebolavirus/metabolismo
Doença pelo Vírus Ebola/virologia
Proteínas Virais Reguladoras e Acessórias/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Transporte/metabolismo
Grânulos Citoplasmáticos/metabolismo
DNA Helicases
Ebolavirus/química
Ebolavirus/genética
Fator de Iniciação 2 em Eucariotos/metabolismo
Fator de Iniciação 3 em Eucariotos/metabolismo
Doença pelo Vírus Ebola/metabolismo
Interações Hospedeiro-Patógeno
Seres Humanos
Proteínas de Ligação a Poli-ADP-Ribose
Ligação Proteica
Domínios Proteicos
RNA Helicases
Proteínas com Motivo de Reconhecimento de RNA
Proteínas Virais Reguladoras e Acessórias/química
Proteínas Virais Reguladoras e Acessórias/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Eukaryotic Initiation Factor-2); 0 (Eukaryotic Initiation Factor-3); 0 (Poly-ADP-Ribose Binding Proteins); 0 (RNA Recognition Motif Proteins); 0 (VP35 protein, filovirus); 0 (Viral Regulatory and Accessory Proteins); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (G3BP1 protein, human); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161226
[St] Status:MEDLINE


  10 / 151 MEDLINE  
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[PMID]:28011649
[Au] Autor:Sun Y; Dong L; Yu S; Wang X; Zheng H; Zhang P; Meng C; Zhan Y; Tan L; Song C; Qiu X; Wang G; Liao Y; Ding C
[Ad] Endereço:Department of Avian Infectious Diseases, Shanghai Veterinary Research Institute, Chinese Academy of Agricultural Science, Shanghai, China.
[Ti] Título:Newcastle disease virus induces stable formation of stress granules to facilitate viral replication through manipulating host protein translation.
[So] Source:FASEB J;31(4):1337-1353, 2017 Apr.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mammalian cells respond to various environmental stressors to form stress granules (SGs) by arresting cytoplasmic mRNA, protein translation element, and RNA binding proteins. Virus-induced SGs function in different ways, depending on the species of virus; however, the mechanism of SG regulation of virus replication is not well understood. In this study, Newcastle disease virus (NDV) triggered stable formation of SGs on HeLa cells through activating the protein kinase R (PKR)/eIF2α pathway. NDV-induced SGs contained classic SG markers T-cell internal antigen (TIA)-1, Ras GTPase-activating protein-binding protein (G3BP)-1, eukaryotic initiation factors, and small ribosomal subunit, which could be disassembled in the presence of cycloheximide. Treatment with nocodazole, a microtubule disruption drug, led to the formation of relatively small and circular granules, indicating that NDV infection induces canonical SGs. Furthermore, the role of SGs on NDV replication was investigated by knockdown of TIA-1 and TIA-1-related (TIAR) protein, the 2 critical components involved in SG formation from the HeLa cells, followed by NDV infection. Results showed that depletion of TIA-1 or TIAR inhibited viral protein synthesis, reduced extracellular virus yields, but increased global protein translation. FISH revealed that NDV-induced SGs contained predominantly cellular mRNA rather than viral mRNA. Deletion of TIA-1 or TIAR reduced NP mRNA levels in polysomes. These results demonstrate that NDV triggers stable formation of SGs, which benefit viral protein translation and virus replication by arresting cellular mRNA.-Sun, Y., Dong, L., Yu, S., Wang, X., Zheng, H., Zhang, P., Meng, C., Zhan, Y., Tan, L., Song, C., Qiu, X., Wang, G., Liao, Y., Ding, C. Newcastle disease virus induces stable formation of stress granules to facilitate viral replication through manipulating host protein translation.
[Mh] Termos MeSH primário: Grânulos Citoplasmáticos/metabolismo
Interações Hospedeiro-Patógeno
Vírus da Doença de Newcastle/fisiologia
Replicação Viral
[Mh] Termos MeSH secundário: Animais
Proteínas de Transporte/metabolismo
Células Cultivadas
Galinhas
DNA Helicases
Fator de Iniciação 2 em Eucariotos/metabolismo
Células HeLa
Seres Humanos
Vírus da Doença de Newcastle/metabolismo
Vírus da Doença de Newcastle/patogenicidade
Proteínas de Ligação a Poli(A)/metabolismo
Proteínas de Ligação a Poli-ADP-Ribose
Biossíntese de Proteínas
RNA Helicases
Proteínas com Motivo de Reconhecimento de RNA
Proteínas de Ligação a RNA
Subunidades Ribossômicas/metabolismo
Antígeno-1 Intracelular de Células T
eIF-2 Quinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Eukaryotic Initiation Factor-2); 0 (Poly(A)-Binding Proteins); 0 (Poly-ADP-Ribose Binding Proteins); 0 (RNA Recognition Motif Proteins); 0 (RNA-Binding Proteins); 0 (T-Cell Intracellular Antigen-1); 0 (TIA1 protein, human); 148592-68-1 (TIAL1 protein, human); EC 2.7.11.1 (eIF-2 Kinase); EC 3.6.4.- (DNA Helicases); EC 3.6.4.12 (G3BP1 protein, human); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201600980R



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