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Pesquisa : D13.444.735.757 [Categoria DeCS]
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[PMID]:29212662
[Au] Autor:Chatterjee K; Majumder S; Wan Y; Shah V; Wu J; Huang HY; Hopper AK
[Ad] Endereço:The Ohio State University Comprehensive Cancer Research Center, The Ohio State University, Columbus, Ohio 43210, USA.
[Ti] Título:Sharing the load: Mex67-Mtr2 cofunctions with Los1 in primary tRNA nuclear export.
[So] Source:Genes Dev;31(21):2186-2198, 2017 11 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic transfer RNAs (tRNAs) are exported from the nucleus, their site of synthesis, to the cytoplasm, their site of function for protein synthesis. The evolutionarily conserved ß-importin family member Los1 (Exportin-t) has been the only exporter known to execute nuclear export of newly transcribed intron-containing pre-tRNAs. Interestingly, is unessential in all tested organisms. As tRNA nuclear export is essential, we previously interrogated the budding yeast proteome to identify candidates that function in tRNA nuclear export. Here, we provide molecular, genetic, cytological, and biochemical evidence that the Mex67-Mtr2 (TAP-p15) heterodimer, best characterized for its essential role in mRNA nuclear export, cofunctions with Los1 in tRNA nuclear export. Inactivation of Mex67 or Mtr2 leads to rapid accumulation of end-matured unspliced tRNAs in the nucleus. Remarkably, merely fivefold overexpression of Mex67-Mtr2 can substitute for Los1 in Δ cells. Moreover, in vivo coimmunoprecipitation assays with tagged Mex67 document that the Mex67 binds tRNAs. Our data also show that tRNA exporters surprisingly exhibit differential tRNA substrate preferences. The existence of multiple tRNA exporters, each with different tRNA preferences, may indicate that the proteome can be regulated by tRNA nuclear export. Thus, our data show that Mex67-Mtr2 functions in primary nuclear export for a subset of yeast tRNAs.
[Mh] Termos MeSH primário: Transporte Ativo do Núcleo Celular/genética
Proteoma/genética
RNA de Transferência/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Inativação Gênica
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/genética
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Proteínas de Transporte Nucleocitoplasmático/genética
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Ligação Proteica
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Los1 protein, S cerevisiae); 0 (MEX67 protein, S cerevisiae); 0 (Membrane Transport Proteins); 0 (Mtr2 protein, S cerevisiae); 0 (Nuclear Pore Complex Proteins); 0 (Nuclear Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (Proteome); 0 (RNA-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1101/gad.305904.117


  2 / 18362 MEDLINE  
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[PMID]:28471404
[Au] Autor:Aubee JI; Olu M; Thompson KM
[Ad] Endereço:Department of Microbiology, College of Medicine, Howard University, Washington, DC 20059, USA. joseph.aubee@howard.edu.
[Ti] Título:TrmL and TusA Are Necessary for rpoS and MiaA Is Required for hfq Expression in Escherichia coli.
[So] Source:Biomolecules;7(2), 2017 May 04.
[Is] ISSN:2218-273X
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Previous work demonstrated that efficient RNA Polymerase sigma S-subunit (RpoS) translation requires the N6-isopentenyladenosine i6A37 transfer RNA (tRNA) modification for UUX-Leu decoding. Here we investigate the effect of two additional tRNA modification systems on RpoS translation; the analysis was also extended to another High UUX-leucine codon (HULC) protein, Host Factor for phage Qß (Hfq). One tRNA modification, the addition of the 2'-O-methylcytidine/uridine 34 (C/U34m) tRNA modification by tRNA (cytidine/uridine-2'O)-ribose methyltransferase L (TrmL), requires the presence of the 6-isopentenyladenosine 37 (i6A37) and therefore it seemed possible that the defect in RpoS translation in the absence of i6A37 prenyl transferase (MiaA) was in fact due to the inability to add the C/U34m modification to UUX-Leu tRNAs. The second modification, addition of 2-thiouridine (s²U), part of (mnm5s²U34), is dependent on tRNA 2-thiouridine synthesizing protein A (TusA), previously shown to affect RpoS levels. We compared expression of P - translational fusions carrying wild-type UUX leucine codons with derivatives in which UUX codons were changed to CUX codons, in the presence and absence of TrmL or TusA. The absence of these proteins, and therefore presumably the modifications they catalyze, both abolished P - - translation activity. UUX-Leu to CUX-Leu codon mutations in suppressed the requirement for P - - expression. Thus, it is likely that the C/U34m and s²U34 tRNA modifications are necessary for full translation. We also measured P - translational fusion activity in the absence of C/U34m ( ) or i6A37 ( ). The absence of i6A37 resulted in decreased P - expression, consistent with a role for i6A37 tRNA modification for translation.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Proteínas de Bactérias/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Fator Proteico 1 do Hospedeiro/genética
Metiltransferases/metabolismo
Fator sigma/metabolismo
[Mh] Termos MeSH secundário: Sequência de Bases
Escherichia coli/genética
RNA de Transferência/genética
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Escherichia coli Proteins); 0 (Hfq protein, E coli); 0 (Host Factor 1 Protein); 0 (Sigma Factor); 0 (TusA protein, E coli); 0 (sigma factor KatF protein, Bacteria); 9014-25-9 (RNA, Transfer); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (TrmL protein, E coli); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.27 (adenylate isopentenyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  3 / 18362 MEDLINE  
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[PMID]:29215639
[Au] Autor:Noller HF; Lancaster L; Zhou J; Mohan S
[Ad] Endereço:Department of Molecular, Cell and Developmental Biology and Center for Molecular Biology of RNA, University of California at Santa Cruz, Santa Cruz, California, USA.
[Ti] Título:The ribosome moves: RNA mechanics and translocation.
[So] Source:Nat Struct Mol Biol;24(12):1021-1027, 2017 Dec 07.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During protein synthesis, mRNA and tRNAs must be moved rapidly through the ribosome while maintaining the translational reading frame. This process is coupled to large- and small-scale conformational rearrangements in the ribosome, mainly in its rRNA. The free energy from peptide-bond formation and GTP hydrolysis is probably used to impose directionality on those movements. We propose that the free energy is coupled to two pawls, namely tRNA and EF-G, which enable two ratchet mechanisms to act separately and sequentially on the two ribosomal subunits.
[Mh] Termos MeSH primário: Bactérias/metabolismo
Biossíntese de Proteínas/fisiologia
RNA Mensageiro/genética
RNA de Transferência/genética
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Bactérias/genética
Modelos Moleculares
Fator G para Elongação de Peptídeos/metabolismo
Conformação Proteica
RNA Mensageiro/metabolismo
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (RNA, Messenger); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3505


  4 / 18362 MEDLINE  
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[PMID]:28467833
[Au] Autor:Bian X; Tang B; Yu Y; Tu Q; Gross F; Wang H; Li A; Fu J; Shen Y; Li YZ; Stewart AF; Zhao G; Ding X; Müller R; Zhang Y
[Ad] Endereço:Shandong University-Helmholtz Institute of Biotechnology, State Key Laboratory of Microbial Technology, School of Life Science, Shandong University , Qingdao 266235, China.
[Ti] Título:Heterologous Production and Yield Improvement of Epothilones in Burkholderiales Strain DSM 7029.
[So] Source:ACS Chem Biol;12(7):1805-1812, 2017 Jul 21.
[Is] ISSN:1554-8937
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cloning of microbial natural product biosynthetic gene clusters and their heterologous expression in a suitable host have proven to be a feasible approach to improve the yield of valuable natural products and to begin mining cryptic natural products in microorganisms. Myxobacteria are a prolific source of novel bioactive natural products with only limited choices of heterologous hosts that have been exploited. Here, we describe the use of Burkholderiales strain DSM 7029 as a potential heterologous host for the functional expression of myxobacterial secondary metabolites. Using a newly established electroporation procedure, the 56 kb epothilone biosynthetic gene cluster from the myxobacterium Sorangium cellulosum was introduced into the chromosome of strain DSM 7029 by transposition. Production of epothilones A, B, C, and D was detected despite their yields being low. Optimization of the medium, introduction of the exogenous methylmalonyl-CoA biosynthetic pathway, and overexpression of rare tRNA genes resulted in an approximately 75-fold increase in the total yields of epothilones to 307 µg L . These results show that strain DSM 7029 has the potential to produce epothilones with reasonable titers and might be a broadly applicable host for the heterologous expression of other myxobacterial polyketide synthases and nonribosomal peptide synthetases, expediting the process of genome mining.
[Mh] Termos MeSH primário: Produtos Biológicos/metabolismo
Epotilonas/biossíntese
Microbiologia Industrial/métodos
Myxococcales/metabolismo
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão
Eletroporação
Epotilonas/química
Epotilonas/genética
Estrutura Molecular
Myxococcales/genética
RNA de Transferência/genética
RNA de Transferência/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biological Products); 0 (Epothilones); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1021/acschembio.7b00097


  5 / 18362 MEDLINE  
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[PMID]:29307851
[Au] Autor:Bai J; Xu S; Nie Z; Wang Y; Zhu C; Wang Y; Min W; Cai Y; Zou J; Zhou X
[Ad] Endereço:Research lab of Freshwater Crustacean Decapoda &Paragonimus, School of Basic Medical Sciences, Nanchang University, 461 Bayi Avenue, Nanchang City, Jiangxi Province 330006, People's Republic of China.
[Ti] Título:The complete mitochondrial genome of Huananpotamon lichuanense (Decapoda: Brachyura) with phylogenetic implications for freshwater crabs.
[So] Source:Gene;646:217-226, 2018 Mar 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In the present study, we determined the complete mitochondrial genome of Huananpotamon lichuanense (Decapoda: Brachyura) for the first time. The genome is 15,380bp in length and typically consists of 37 genes. When the gene order was compared to the ancestral crustacean type, two tRNA genes (tRNA and tRNA ) were rearranged in H. lichuanense, and the translocation of tRNA appeared only in Potamoidea crabs, such as Geothelphusa dehaani and Sinopotamon xiushuiense, supporting the monophyly of the Potamoidea superfamily. Thirteen protein-coding genes and 2 rRNA genes were divided into five complexes to perform the phylogenetic analysis, and the results showed that the trees constructed by complex I (ND1-ND6 and ND4L), complex IV (COX1-COX3) and rRNA genes better accord with the morphological classification system, suggesting that molecular markers of higher-level phylogeny can be developed in these three complexes in the future. The estimated divergence time for freshwater crabs is approximately 133.58Ma, and G. dehaani from Japan diverged from the freshwater crabs of mainland China approximately 60.66Ma. A selective pressure analysis based on current data revealed obviously increasing dN/dS ratios (except for ATP6 and ND4L) of freshwater crabs, and the accumulation of nonsynonymous mutations suggests that terrestrial habitats provide a relatively relaxed selective pressure environment for this group.
[Mh] Termos MeSH primário: Braquiúros/genética
Genoma Mitocondrial
Mitocôndrias/genética
Análise de Sequência de DNA/métodos
[Mh] Termos MeSH secundário: Animais
Evolução Molecular
Ordem dos Genes
Tamanho do Genoma
Masculino
Filogenia
RNA de Transferência/genética
Seleção Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


  6 / 18362 MEDLINE  
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[PMID]:28461681
[Au] Autor:Wise JA; Nielsen O
[Ad] Endereço:Center for RNA Molecular Biology and Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106-4906 jaw17@case.edu.
[Ti] Título:Analysis of RNA Metabolism in Fission Yeast.
[So] Source:Cold Spring Harb Protoc;2017(5):pdb.top079798, 2017 May 01.
[Is] ISSN:1559-6095
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Here we focus on the biogenesis and function of messenger RNA (mRNA) in fission yeast cells. Following a general introduction that also briefly touches on other classes of RNA, we provide an overview of methods used to analyze mRNAs throughout their life cycles.
[Mh] Termos MeSH primário: RNA Fúngico/metabolismo
Schizosaccharomyces/genética
[Mh] Termos MeSH secundário: Biossíntese de Proteínas
Processamento de RNA
RNA Mensageiro/metabolismo
RNA Ribossômico/metabolismo
RNA Interferente Pequeno/metabolismo
RNA Nucleolar Pequeno/metabolismo
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Fungal); 0 (RNA, Messenger); 0 (RNA, Ribosomal); 0 (RNA, Small Interfering); 0 (RNA, Small Nucleolar); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1101/pdb.top079798


  7 / 18362 MEDLINE  
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[PMID]:25815561
[Au] Autor:Wang XC; Wu K; Chen H; Shao J; Zhang N; Chen X; Lan J; Liu C
[Ad] Endereço:a Institute of Medicinal Plant Development, Chinese Academy of Medical Science , Beijing , PR China.
[Ti] Título:The complete mitochondrial genome of the white-rot fungus Ganoderma meredithiae (Polyporales, Basidiomycota).
[So] Source:Mitochondrial DNA A DNA Mapp Seq Anal;27(6):4197-4198, 2016 Nov.
[Is] ISSN:2470-1408
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Complete nucleotide sequence of the 78,447 bp mitochondrial genome of the white-rotting fungus Ganoderma meredithiae Adask. & Gilb. has been determined by next-generation sequencing technology. The circular molecule encodes a set of mitochondrial protein and RNA genes, including 15 conserved proteins, 29 tRNAs, large and small ribosomal RNAs, and 18 homing endonucleases, with a GC content of 26.14%. All structural genes are located on the same strand except trnW-CCA. Compared with previously sequenced mtDNAs of G. lucidum and G. sinense, the gene order of protein and rRNA genes among the three mitogenomes is highly conserved; however, the tRNA composition is slightly different. The mitochondrial genome of G. meredithiae will contribute to understanding the phylogeny and evolution of Ganoderma and Ganodermataceae, the group containing many species with high medicinal values.
[Mh] Termos MeSH primário: Ganoderma/genética
Genoma Mitocondrial/genética
[Mh] Termos MeSH secundário: DNA Mitocondrial/genética
Proteínas Fúngicas/genética
Proteínas Mitocondriais/genética
RNA/genética
RNA Fúngico/genética
RNA Ribossômico/genética
RNA de Transferência/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Fungal Proteins); 0 (Mitochondrial Proteins); 0 (RNA, Fungal); 0 (RNA, Ribosomal); 0 (RNA, mitochondrial); 63231-63-0 (RNA); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150328
[St] Status:MEDLINE


  8 / 18362 MEDLINE  
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[PMID]:29227991
[Au] Autor:Sonney S; Leipzig J; Lott MT; Zhang S; Procaccio V; Wallace DC; Sondheimer N
[Ad] Endereço:Division of Clinical and Metabolic Genetics, The Hospital for Sick Children, Toronto, Ontario, Canada.
[Ti] Título:Predicting the pathogenicity of novel variants in mitochondrial tRNA with MitoTIP.
[So] Source:PLoS Comput Biol;13(12):e1005867, 2017 12.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Novel or rare variants in mitochondrial tRNA sequences may be observed after mitochondrial DNA analysis. Determining whether these variants are pathogenic is critical, but confirmation of the effect of a variant on mitochondrial function can be challenging. We have used available databases of benign and pathogenic variants, alignment between diverse tRNAs, structural information and comparative genomics to predict the impact of all possible single-base variants and deletions. The Mitochondrial tRNA Informatics Predictor (MitoTIP) is available through MITOMAP at www.mitomap.org. The source code for MitoTIP is available at www.github.com/sonneysa/MitoTIP.
[Mh] Termos MeSH primário: Mitocôndrias/genética
RNA de Transferência/genética
Virulência
[Mh] Termos MeSH secundário: Conformação de Ácido Nucleico
RNA de Transferência/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180111
[Lr] Data última revisão:
180111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005867


  9 / 18362 MEDLINE  
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[PMID]:28449100
[Au] Autor:Villada JC; Brustolini OJB; Batista da Silveira W
[Ad] Endereço:Department of Microbiology, Universidade Federal de Viçosa, Viçosa 36570-900, Brazil.
[Ti] Título:Integrated analysis of individual codon contribution to protein biosynthesis reveals a new approach to improving the basis of rational gene design.
[So] Source:DNA Res;24(4):419-434, 2017 Aug 01.
[Is] ISSN:1756-1663
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Gene codon optimization may be impaired by the misinterpretation of frequency and optimality of codons. Although recent studies have revealed the effects of codon usage bias (CUB) on protein biosynthesis, an integrated perspective of the biological role of individual codons remains unknown. Unlike other previous studies, we show, through an integrated framework that attributes of codons such as frequency, optimality and positional dependency should be combined to unveil individual codon contribution for protein biosynthesis. We designed a codon quantification method for assessing CUB as a function of position within genes with a novel constraint: the relativity of position-dependent codon usage shaped by coding sequence length. Thus, we propose a new way of identifying the enrichment, depletion and non-uniform positional distribution of codons in different regions of yeast genes. We clustered codons that shared attributes of frequency and optimality. The cluster of non-optimal codons with rare occurrence displayed two remarkable characteristics: higher codon decoding time than frequent-non-optimal cluster and enrichment at the 5'-end region, where optimal codons with the highest frequency are depleted. Interestingly, frequent codons with non-optimal adaptation to tRNAs are uniformly distributed in the Saccharomyces cerevisiae genes, suggesting their determinant role as a speed regulator in protein elongation.
[Mh] Termos MeSH primário: Códon
Biossíntese de Proteínas
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: RNA Fúngico/metabolismo
RNA de Transferência/metabolismo
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (RNA, Fungal); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180109
[Lr] Data última revisão:
180109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/dnares/dsx014


  10 / 18362 MEDLINE  
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[PMID]:29211986
[Au] Autor:Jamiolkowski RM; Chen C; Cooperman BS; Goldman YE
[Ad] Endereço:Pennsylvania Muscle Institute, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania.
[Ti] Título:tRNA Fluctuations Observed on Stalled Ribosomes Are Suppressed during Ongoing Protein Synthesis.
[So] Source:Biophys J;113(11):2326-2335, 2017 Dec 05.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pretranslocation complex of the ribosome can undergo spontaneous fluctuations of messenger RNA and transfer RNAs (tRNAs) between classical and hybrid states, and occupation of the hybrid tRNA positions has been proposed to precede translocation. The classical and hybrid state tRNA positions have been extensively characterized when the ribosome is stalled along the messenger RNA by either the absence or delayed addition of elongation factor G (EF-G), or by the presence of antibiotics or GTP analogs that block translocation. However, during multiple ongoing elongation cycles when both EF-G and ternary complexes are present, EF-G can bind to the pretranslocation complex much faster than the timescale of the classic-hybrid transitions. Using single-molecule fluorescence resonance energy transfer between adjacent tRNAs and between A-site tRNA and ribosomal protein L11, we found that the tRNAs do not fluctuate between the hybrid and classical states, but instead adopt a position with fluorescence resonance energy transfer efficiencies between those of the stalled classical and hybrid states.
[Mh] Termos MeSH primário: Biossíntese de Proteínas
RNA de Transferência/genética
Ribossomos/genética
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Transferência Ressonante de Energia de Fluorescência
Fator G para Elongação de Peptídeos/metabolismo
Proteínas Ribossômicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (Ribosomal Proteins); 0 (ribosomal protein L11); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE



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