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[PMID]:29381712
[Au] Autor:Gallie DR
[Ad] Endereço:Department of Biochemistry, University of California, Riverside, CA, United States of America.
[Ti] Título:Plant growth and fertility requires functional interactions between specific PABP and eIF4G gene family members.
[So] Source:PLoS One;13(1):e0191474, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The initiation of protein synthesis requires the involvement of the eukaryotic translation initiation factor (eIF) 4G to promote assembly of the factors needed to recruit a 40S ribosomal subunit to an mRNA. Although many eukaryotes express two eIF4G isoforms that are highly similar, those in plants, referred to as eIF4G and eIFiso4G, are highly divergent in size, sequence, and domain organization. Species of the Brassicaceae and the Cleomaceae also express a divergent eIFiso4G isoform, referred to as eIFiso4G2, not found elsewhere in the plant kingdom. Despite their divergence, eIF4G and eIFiso4G interact with eIF4A, eIF4B, and eIF4E isoforms needed for binding an mRNA. eIF4G and eIFiso4G also interact with the poly(A)-binding protein (PABP) which promotes ribosome recruitment to an mRNA. Increasing the complexity of such an interaction, however, Arabidopsis also expresses three PABP isoforms (PAB2, PAB4, and PAB8) in vegetative and reproductive tissues. In this study, the functional interactions among the eIF4G and the widely-expressed PABP isoforms were examined. Loss of PAB2 or PAB8 in combination with loss of eIF4G or eIFiso4G had little to no effect on growth or fertility whereas pab2 pab8 eif4g or pab2 pab8 eifiso4g1/2 mutants exhibited smaller stature and reduced fertility. Although the pab4 eifiso4g1 mutant grows normally and is fertile, pab4 eif4g or pab4 eifiso4g2 mutants could not be isolated. Even pab4/PAB4 eif4g/eIF4G heterozygous plants exhibited growth defects and low fertility. Mutant co-inheritance analysis in reciprocal crosses with wild-type plants revealed that most ovaries and pollen from pab4/PAB4 eif4g/eIF4G plants were PAB4 eif4g. Similarly, co-inheritance studies with pab4/PAB4 eifiso4g2/eIFiso4G2 plants suggested most ovaries were PAB4 eifiso4g2. These results suggest that a functional interaction between PAB4 and eIF4G and between PAB4 and eIFiso4G2 is required for growth and normal fertility.
[Mh] Termos MeSH primário: Arabidopsis/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Fertilidade
Desenvolvimento Vegetal
Proteínas de Plantas/fisiologia
Proteínas de Ligação a Poli(A)/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Plantas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Eukaryotic Initiation Factor-4G); 0 (Plant Proteins); 0 (Poly(A)-Binding Proteins)
[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:180131
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191474


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[PMID]:27773676
[Au] Autor:Grüner S; Peter D; Weber R; Wohlbold L; Chung MY; Weichenrieder O; Valkov E; Igreja C; Izaurralde E
[Ad] Endereço:Department of Biochemistry, Max Planck Institute for Developmental Biology, Spemannstrasse 35, 72076 Tübingen, Germany.
[Ti] Título:The Structures of eIF4E-eIF4G Complexes Reveal an Extended Interface to Regulate Translation Initiation.
[So] Source:Mol Cell;64(3):467-479, 2016 Nov 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic initiation factor 4G (eIF4G) plays a central role in translation initiation through its interactions with the cap-binding protein eIF4E. This interaction is a major drug target for repressing translation and is naturally regulated by 4E-binding proteins (4E-BPs). 4E-BPs and eIF4G compete for binding to the eIF4E dorsal surface via a shared canonical 4E-binding motif, but also contain auxiliary eIF4E-binding sequences, which were assumed to contact non-overlapping eIF4E surfaces. However, it is unknown how metazoan eIF4G auxiliary sequences bind eIF4E. Here, we describe crystal structures of human and Drosophila melanogaster eIF4E-eIF4G complexes, which unexpectedly reveal that the eIF4G auxiliary sequences bind to the lateral surface of eIF4E, using a similar mode to that of 4E-BPs. Our studies provide a molecular model of the eIF4E-eIF4G complex, shed light on the competition mechanism of 4E-BPs, and enable the rational design of selective eIF4G inhibitors to dampen dysregulated translation in disease.
[Mh] Termos MeSH primário: Drosophila melanogaster/metabolismo
Fator de Iniciação 4E em Eucariotos/química
Fator de Iniciação 4G em Eucariotos/química
Iniciação Traducional da Cadeia Peptídica
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Clonagem Molecular
Cristalografia por Raios X
Drosophila melanogaster/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Fator de Iniciação 4E em Eucariotos/genética
Fator de Iniciação 4E em Eucariotos/metabolismo
Fator de Iniciação 4G em Eucariotos/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Expressão Gênica
Seres Humanos
Cinética
Modelos Moleculares
Mutação
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eukaryotic Initiation Factor-4E); 0 (Eukaryotic Initiation Factor-4G); 0 (Recombinant Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180114
[Lr] Data última revisão:
180114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status: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


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[PMID]:27771839
[Au] Autor:Cheng F; Zhao J; Hanker AB; Brewer MR; Arteaga CL; Zhao Z
[Ad] Endereço:Department of Biomedical Informatics, Vanderbilt University Medical Center, Nashville, TN, 37203, USA.
[Ti] Título:Transcriptome- and proteome-oriented identification of dysregulated eIF4G, STAT3, and Hippo pathways altered by PIK3CA in HER2/ER-positive breast cancer.
[So] Source:Breast Cancer Res Treat;160(3):457-474, 2016 12.
[Is] ISSN:1573-7217
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Phosphatidylinositol 3-kinase (PI3K)/AKT pathway aberrations are common in human breast cancer. Furthermore, PIK3CA mutations are commonly associated with resistance to anti-epidermal growth factor receptor 2 (HER2) or anti-estrogen receptor (ER) agents in HER2 or ER positive (HER2 /ER ) breast cancer. Hence, deciphering the underlying mechanisms of PIK3CA mutations in HER2 /ER breast cancer would provide novel insights into elucidating resistance to anti-HER2/ER therapies. METHODS: In this study, we systematically investigated the biological consequences of PIK3CA in HER2 /ER breast cancer by uniquely incorporating mRNA transcriptomic data from The Cancer Genome Atlas and proteomic data from reverse-phase protein arrays. RESULTS: Our integrative bioinformatics analyses revealed that several important pathways such as STAT3 and VEGF/hypoxia were selectively altered by PIK3CA in HER2 /ER breast cancer. Protein differential expression analysis indicated that an elevated eIF4G might promote tumor angiogenesis and growth via regulation of the hypoxia-activated switch in HER2 PIK3CA breast cancer. We observed hypo-phosphorylation of EGFR in HER2 PIK3CA breast cancer versus HER2 PIK3CA (PIK3CA ). In addition, ER and PIK3CA might cooperate to activate STAT3, MAPK, AKT, and Hippo pathways in ER PIK3CA breast cancer. A higher YAP level was observed in ER PIK3CA patients than that in an ER PIK3CA subgroup. By examining breast cancer cell lines having both microarray gene expression and drug treatment data from the Genomics of Drug Sensitivity in Cancer and the Stand Up to Cancer datasets, we found that the elevated YAP1 mRNA expression was associated with the resistance of BCL-2 family inhibitors, but with the sensitivity to MEK/MAPK inhibitors in breast cancer cells. CONCLUSIONS: In summary, these findings shed light on the functional consequences of PIK3CA -driven breast tumorigenesis and resistance to the existing therapeutic agents in HER2 /ER breast cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Neoplasias da Mama/metabolismo
Classe I de Fosfatidilinositol 3-Quinases/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Receptor ErbB-2/genética
Receptores Estrogênicos/genética
Fator de Transcrição STAT3/metabolismo
[Mh] Termos MeSH secundário: Biomarcadores
Neoplasias da Mama/tratamento farmacológico
Neoplasias da Mama/patologia
Linhagem Celular Tumoral
Transformação Celular Neoplásica/genética
Transformação Celular Neoplásica/metabolismo
Análise por Conglomerados
Biologia Computacional/métodos
Bases de Dados Genéticas
Resistência a Medicamentos Antineoplásicos/genética
Feminino
Perfilação da Expressão Gênica/métodos
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Terapia de Alvo Molecular
Mutação
Fosforilação
Proteômica/métodos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Biomarkers); 0 (Eukaryotic Initiation Factor-4G); 0 (Receptors, Estrogen); 0 (STAT3 Transcription Factor); EC 2.7.1.137 (Class I Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (PIK3CA protein, human); EC 2.7.10.1 (Receptor, ErbB-2); EC 2.7.11.1 (Hippo protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171209
[Lr] Data última revisão:
171209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE
[do] DOI:10.1007/s10549-016-4011-9


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[PMID]:28934492
[Au] Autor:Du Z; Alekhina OM; Vassilenko KS; Simon AE
[Ad] Endereço:Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, MD 20742, USA.
[Ti] Título:Concerted action of two 3' cap-independent translation enhancers increases the competitive strength of translated viral genomes.
[So] Source:Nucleic Acids Res;45(16):9558-9572, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Several families of plant viruses evolved cap-independent translation enhancers (3'CITE) in the 3' untranslated regions of their genomic (g)RNAs to compete with ongoing cap-dependent translation of cellular mRNAs. Umbravirus Pea enation mosaic virus (PEMV)2 is the only example where three 3'CITEs enhance translation: the eIF4E-binding Panicum mosaic virus-like translational enhancer (PTE) and ribosome-binding 3' T-shaped structure (TSS) have been found in viruses of different genera, while the ribosome-binding kl-TSS that provides a long-distance interaction with the 5' end is unique. We report that the PTE is the key translation promoting element, but inhibits translation in cis and in trans in the absence of the kl-TSS by sequestering initiation factor eIF4G. PEMV2 strongly outcompeted a cellular mRNA mimic for translation, indicating that the combination of kl-TSS and PTE is highly efficient. Transferring the 3'-5' interaction from the kl-TSS to the PTE (to fulfill its functionality as found in other viruses) supported translationin vitro, but gRNA did not accumulate to detectable levels in protoplasts in the absence of the kl-TSS. It was shown that the PTE in conjunction with the kl-TSS did not markedly affect the translation initiation rate but rather increased the number of gRNAs available for translation. A model is proposed to explain how 3'CITE-based regulation of ribosome recruitment enhances virus fitness.
[Mh] Termos MeSH primário: Elementos Facilitadores Genéticos
Genoma Viral
Luteoviridae/genética
Capuzes de RNA/genética
[Mh] Termos MeSH secundário: Arabidopsis/virologia
Códon de Iniciação
Fator de Iniciação 4G em Eucariotos/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Luteoviridae/metabolismo
Polirribossomos/metabolismo
Biossíntese de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Initiator); 0 (Eukaryotic Initiation Factor-4G); 0 (RNA Caps)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx643


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[PMID]:28843814
[Au] Autor:Aumayr M; Schrempf A; Üzülmez Ö; Olek KM; Skern T
[Ad] Endereço:Max F. Perutz Laboratories, Medical University of Vienna, Dept. of Medical Biochemistry, Vienna Biocenter, Dr. Bohr-Gasse 9/3, A-1030 Vienna, Austria.
[Ti] Título:Interaction of 2A proteinase of human rhinovirus genetic group A with eIF4E is required for eIF4G cleavage during infection.
[So] Source:Virology;511:123-134, 2017 Nov.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In enteroviruses, the inhibition of protein synthesis from capped host cell mRNA is catalyzed by the virally encoded 2A proteinase (2A ), which cleaves eukaryotic initiation factors (eIF) 4GI and 4GII. Despite much investigation, the exact mechanism of 2A cleavage remains however unclear. Here, we identify the domains responsible for the eIF4E/HRV2 2A interaction using molecular modelling and describe mutations that impair this interaction and delay in vitro cleavage of eIF4G isoforms. Furthermore, we produced HRV1A viruses bearing the mutation L17R, Y32A or Y86A in the 2A sequence. All three viruses showed reduced yield and were appreciably delayed during infection in eIF4GI cleavage. Thus, we propose for genetic group A HRVs that the eIF4E/2A interaction is essential for successful viral replication. In contrast, HRV4 2A and coxsackievirus B4 2A failed to form complexes with eIF4E, suggesting that the mechanism of eIF4G isoform cleavage in these and related viruses is different.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/metabolismo
Fator de Iniciação 4E em Eucariotos/metabolismo
Fator de Iniciação 4G em Eucariotos/metabolismo
Interações Hospedeiro-Patógeno
Mapeamento de Interação de Proteínas
Rhinovirus/enzimologia
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Análise Mutacional de DNA
Genótipo
Seres Humanos
Hidrólise
Modelos Moleculares
Ligação Proteica
Rhinovirus/genética
Rhinovirus/patogenicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EIF4G1 protein, human); 0 (Eukaryotic Initiation Factor-4E); 0 (Eukaryotic Initiation Factor-4G); 0 (Viral Proteins); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.29 (picornain 2A, Picornavirus)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170828
[St] Status:MEDLINE


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[PMID]:28738064
[Au] Autor:Contreras-Treviño HI; Reyna-Rosas E; León-Rodríguez R; Ruiz-Ordaz BH; Dinkova TD; Cevallos AM; Padilla-Noriega L
[Ad] Endereço:Programa de Maestría y Doctorado en Ciencias Bioquímicas, Universidad Nacional Autónoma de México, Mexico City, Mexico.
[Ti] Título:Species A rotavirus NSP3 acquires its translation inhibitory function prior to stable dimer formation.
[So] Source:PLoS One;12(7):e0181871, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Species A rotavirus non-structural protein 3 (NSP3) is a translational regulator that inhibits or, under some conditions, enhances host cell translation. NSP3 binds to the translation initiation factor eIF4G1 and evicts poly-(A) binding protein (PABP) from eIF4G1, thus inhibiting translation of polyadenylated mRNAs, presumably by disrupting the effect of PABP bound to their 3'-ends. NSP3 has a long coiled-coil region involved in dimerization that includes a chaperone Hsp90-binding domain (HS90BD). We aimed to study the role in NSP3 dimerization of a segment of the coiled-coil region adjoining the HS90BD. We used a vaccinia virus system to express NSP3 with point mutations in conserved amino acids in the coiled-coil region and determined the effects of these mutations on translation by metabolic labeling of proteins as well as on accumulation of stable NSP3 dimers by non-dissociating Western blot, a method that separates stable NSP3 dimers from the monomer/dimerization intermediate forms of the protein. Four of five mutations reduced the total yield of NSP3 and the formation of stable dimers (W170A, K171E, R173E and R187E:K191E), whereas one mutation had the opposite effects (Y192A). Treatment with the proteasome inhibitor MG132 revealed that stable NSP3 dimers and monomers/dimerization intermediates are susceptible to proteasome degradation. Surprisingly, mutants severely impaired in the formation of stable dimers were still able to inhibit host cell translation, suggesting that NSP3 dimerization intermediates are functional. Our results demonstrate that rotavirus NSP3 acquires its function prior to stable dimer formation and remain as a proteasome target throughout dimerization.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Biossíntese de Proteínas/genética
Multimerização Proteica/genética
Proteínas não Estruturais Virais/genética
Proteínas não Estruturais Virais/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação/genética
Linhagem Celular
Cercopithecus aethiops
Fator de Iniciação 4G em Eucariotos/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Mutação Puntual/genética
Proteínas de Ligação a Poli(A)/genética
Ligação Proteica/genética
RNA Mensageiro/genética
RNA Viral/genética
Rotavirus/genética
Infecções por Rotavirus/virologia
Alinhamento de Sequência
Replicação Viral/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Eukaryotic Initiation Factor-4G); 0 (Poly(A)-Binding Proteins); 0 (RNA, Messenger); 0 (RNA, Viral); 0 (Viral Nonstructural Proteins)
[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:170725
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181871


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[PMID]:28546148
[Au] Autor:Zinshteyn B; Rojas-Duran MF; Gilbert WV
[Ad] Endereço:Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
[Ti] Título:Translation initiation factor eIF4G1 preferentially binds yeast transcript leaders containing conserved oligo-uridine motifs.
[So] Source:RNA;23(9):1365-1375, 2017 Sep.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Translational control of gene expression plays essential roles in cellular stress responses and organismal development by enabling rapid, selective, and localized control of protein production. Translational regulation depends on context-dependent differences in the protein output of mRNAs, but the key mRNA features that distinguish efficiently translated mRNAs are largely unknown. Here, we comprehensively determined the RNA-binding preferences of the eukaryotic initiation factor 4G (eIF4G) to assess whether this core translation initiation factor has intrinsic sequence preferences that may contribute to preferential translation of specific mRNAs. We identified a simple RNA sequence motif-oligo-uridine-that mediates high-affinity binding to eIF4G in vitro. Oligo(U) motifs occur naturally in the transcript leader (TL) of hundreds of yeast genes, and mRNAs with unstructured oligo(U) motifs were enriched in immunoprecipitations against eIF4G. Ribosome profiling following depletion of eIF4G in vivo showed preferentially reduced translation of mRNAs with long TLs, including those that contain oligo(U). Finally, TL oligo(U) elements are enriched in genes with regulatory roles and are conserved between yeast species, consistent with an important cellular function. Taken together, our results demonstrate RNA sequence preferences for a general initiation factor, which cells potentially exploit for translational control of specific mRNAs.
[Mh] Termos MeSH primário: Sítios de Ligação
Fator de Iniciação 4G em Eucariotos/metabolismo
Regulação Fúngica da Expressão Gênica
Motivos de Nucleotídeos
Poli U/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Mh] Termos MeSH secundário: Sequência Conservada
Ligação Proteica
Biossíntese de Proteínas
RNA Mensageiro/química
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eukaryotic Initiation Factor-4G); 0 (RNA, Messenger); 27416-86-0 (Poly U)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1261/rna.062059.117


  9 / 734 MEDLINE  
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[PMID]:28242763
[Au] Autor:Zhao P; Liu Q; Miller WA; Goss DJ
[Ad] Endereço:From the Biochemistry and Chemistry Graduate Programs, Graduate Center, and.
[Ti] Título:Eukaryotic translation initiation factor 4G (eIF4G) coordinates interactions with eIF4A, eIF4B, and eIF4E in binding and translation of the barley yellow dwarf virus 3' cap-independent translation element (BTE).
[So] Source:J Biol Chem;292(14):5921-5931, 2017 Apr 07.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Barley yellow dwarf virus RNA, lacking a 5' cap and a 3' poly(A) tail, contains a cap-independent translation element (BTE) in the 3'-untranslated region that interacts with host translation initiation factor eIF4G. To determine how eIF4G recruits the mRNA, three eIF4G deletion mutants were constructed: (i) eIF4G601-1196, containing amino acids 601-1196, including the putative BTE-binding region, and binding domains for eIF4E, eIF4A, and eIF4B; (ii) eIF4G601-1488, which contains an additional C-terminal eIF4A-binding domain; and (iii) eIF4G742-1196, which lacks the eIF4E-binding site. eIF4G601-1196 binds BTE tightly and supports efficient translation. The helicase complex, consisting of eIF4A, eIF4B, and ATP, stimulated BTE binding with eIF4G601-1196 but not eIF4G601-1488, suggesting that the eIF4A binding domains may serve a regulatory role, with the C-terminal binding site having negative effects. eIF4E binding to eIF4G601-1196 induced a conformational change, significantly increasing the binding affinity to BTE. A comparison of the binding of eIF4G deletion mutants with BTEs containing mutations showed a general correlation between binding affinity and ability to facilitate translation. In summary, these results reveal a new role for the helicase complex in 3' cap-independent translation element-mediated translation and show that the functional core domain of eIF4G plus an adjacent probable RNA-binding domain mediate translation initiation.
[Mh] Termos MeSH primário: Fator de Iniciação 4A em Eucariotos/metabolismo
Fator de Iniciação 4E em Eucariotos/metabolismo
Fator de Iniciação 4G em Eucariotos/metabolismo
Fatores de Iniciação em Eucariotos/metabolismo
Luteovirus/metabolismo
Biossíntese de Proteínas/fisiologia
RNA Helicases/metabolismo
RNA Viral/metabolismo
Proteínas Virais/biossíntese
[Mh] Termos MeSH secundário: Fator de Iniciação 4A em Eucariotos/genética
Fator de Iniciação 4E em Eucariotos/genética
Fator de Iniciação 4G em Eucariotos/genética
Fatores de Iniciação em Eucariotos/genética
Luteovirus/genética
RNA Helicases/genética
RNA Viral/genética
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eukaryotic Initiation Factor-4E); 0 (Eukaryotic Initiation Factor-4G); 0 (Eukaryotic Initiation Factors); 0 (RNA, Viral); 0 (Viral Proteins); 0 (eIF-4B); EC 2.7.7.- (Eukaryotic Initiation Factor-4A); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170301
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.764902


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[PMID]:28131007
[Au] Autor:Woo HH; Lee SC; Gibson SJ; Chambers SK
[Ad] Endereço:University of Arizona Cancer Center, Tucson, AZ 85724, USA. Electronic address: hhwoo@email.arizona.edu.
[Ti] Título:Expression of the cytoplasmic nucleolin for post-transcriptional regulation of macrophage colony-stimulating factor mRNA in ovarian and breast cancer cells.
[So] Source:Biochim Biophys Acta;1860(3):337-348, 2017 03.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The formation of the mRNP complex is a critical component of translational regulation and mRNA decay. Both the 5' and 3'UTRs of CSF-1 mRNA are involved in post-transcriptional regulation. In CSF-1 mRNA, a small hairpin loop structure is predicted to form at the extreme 5' end (2-21nt) of the 5'UTR. Nucleolin binds the hairpin loop structure in the 5'UTR of CSF-1 mRNA and enhances translation, while removal of this hairpin loop nucleolin binding element dramatically represses translation. Thus in CSF-1 mRNA, the hairpin loop nucleolin binding element is critical for translational regulation. In addition, nucleolin interacts with the 3'UTR of CSF-1 mRNA and facilitates the miRISC formation which results in poly (A) tail shortening. The overexpression of nucleolin increases the association of CSF-1 mRNA containing short poly (A) , with polyribosomes. Nucleolin both forms an mRNP complex with the eIF4G and CSF-1 mRNA, and is co-localized with the eIF4G in the cytoplasm further supporting nucleolin's role in translational regulation. The distinct foci formation of nucleolin in the cytoplasm of ovarian and breast cancer cells implicates the translational promoting role of nucleolin in these cancers.
[Mh] Termos MeSH primário: Regiões 5´ não Traduzidas
Neoplasias da Mama/metabolismo
Regulação Neoplásica da Expressão Gênica
Fator Estimulador de Colônias de Macrófagos/biossíntese
Proteínas de Neoplasias/biossíntese
Conformação de Ácido Nucleico
Neoplasias Ovarianas/metabolismo
Fosfoproteínas/biossíntese
Biossíntese de Proteínas
RNA Neoplásico/metabolismo
Proteínas de Ligação a RNA/biossíntese
[Mh] Termos MeSH secundário: Neoplasias da Mama/genética
Linhagem Celular Tumoral
Fator de Iniciação 4G em Eucariotos/genética
Fator de Iniciação 4G em Eucariotos/metabolismo
Feminino
Seres Humanos
Fator Estimulador de Colônias de Macrófagos/genética
Proteínas de Neoplasias/genética
Neoplasias Ovarianas/genética
Fosfoproteínas/genética
Polirribossomos/genética
Polirribossomos/metabolismo
RNA Neoplásico/genética
Proteínas de Ligação a RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (EIF4G1 protein, human); 0 (Eukaryotic Initiation Factor-4G); 0 (Neoplasm Proteins); 0 (Phosphoproteins); 0 (RNA, Neoplasm); 0 (RNA-Binding Proteins); 0 (nucleolin); 81627-83-0 (Macrophage Colony-Stimulating Factor)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE



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