Base de dados : MEDLINE
Pesquisa : D12.776.835.862 [Categoria DeCS]
Referências encontradas : 1503 [refinar]
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  1 / 1503 MEDLINE  
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[PMID]:28467675
[Au] Autor:Urakov VN; Mitkevich OV; Safenkova IV; Ter-Avanesyan MD
[Ad] Endereço:Federal Research Center 'Fundamentals of Biotechnology' of the Russian Academy of Sciences, Bach Institute of Biochemistry, Moscow, Russia.
[Ti] Título:Ribosome-bound Pub1 modulates stop codon decoding during translation termination in yeast.
[So] Source:FEBS J;284(12):1914-1930, 2017 06.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In eukaryotes, termination of translation is controlled by polypeptide chain release factors eRF1 and eRF3, of which the former recognizes nonsense codons, while the latter interacts with eRF1 and stimulates polypeptide release from the ribosome in a GTP- dependent manner, and ABCE1, which facilitates ribosome recycling. In this work, we demonstrate that Pub1, a yeast protein known to be involved in stress granule formation, regulation of gene expression, and organization of the tubulin cytoskeleton, also plays a role in translation termination. Pub1 was shown to bind to ribosomes independent of eRF1 and eRF3 and to interact with the N-terminal glutamine-/asparagine-rich prion domain of eRF3 via its short C-terminal glutamine-rich tract. High velocity sedimentation in sucrose gradient demonstrated that Pub1 was preferentially associated with heavy polysomes enriched with terminating ribosomes. Lack of Pub1 decreased efficiency of nonsense readthrough at a majority but not all tetranucleotide stop signals. This distinguishes Pub1 from most other known binding partners of the release factors which were shown to modulate readthrough of all nonsense codons uniformly. The obtained data show that Pub1 can act as an accessory translation factor involved in fine-tuning of translation termination.
[Mh] Termos MeSH primário: Fatores de Terminação de Peptídeos/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
Ribossomos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Códon de Terminação
Terminação Traducional da Cadeia Peptídica
Fatores de Terminação de Peptídeos/genética
Proteínas de Ligação a Poli(A)/genética
Ribossomos/genética
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/crescimento & desenvolvimento
Proteínas de Saccharomyces cerevisiae/genética
Deleção de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Codon, Terminator); 0 (PUB1 protein, S cerevisiae); 0 (Peptide Termination Factors); 0 (Poly(A)-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (peptide-chain-release factor 3)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14099


  2 / 1503 MEDLINE  
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[PMID]:28743745
[Au] Autor:Korkmaz G; Sanyal S
[Ad] Endereço:From the Department of Cell and Molecular Biology, Uppsala University, Box-596, 75124 Uppsala, Sweden.
[Ti] Título:R213I mutation in release factor 2 (RF2) is one step forward for engineering an omnipotent release factor in bacteria .
[So] Source:J Biol Chem;292(36):15134-15142, 2017 09 08.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The current understanding of the specificity of the bacterial class I release factors (RFs) in decoding stop codons has evolved beyond a simple tripeptide anticodon model. A recent molecular dynamics study for deciphering the principles for specific stop codon recognition by RFs identified Arg-213 as a crucial residue on RF2 for discriminating guanine in the third position (G3). Interestingly, Arg-213 is highly conserved in RF2 and substituted by Ile-196 in the corresponding position in RF1. Another similar pair is Leu-126 in RF1 and Asp-143 in RF2, which are also conserved within their respective groups. With the hypothesis that replacement of Arg-213 and Asp-143 with the corresponding RF1 residues will reduce G3 discrimination by RF2, we swapped these residues between RF1 and RF2 by site-directed mutagenesis and characterized their preference for different codons using a competitive peptide release assay. Among these, the R213I mutant of RF2 showed 5-fold improved reading of the RF1-specific UAG codon relative to UAA, the universal stop codon, compared with the wild type (WT). In-depth fast kinetic studies revealed that the gain in UAG reading by RF2 R213I is associated with a reduced efficiency of termination on the cognate UAA codon. Our work highlights the notion that stop codon recognition involves complex interactions with multiple residues beyond the P T/SPF motifs. We propose that the R213I mutation in RF2 brings us one step forward toward engineering an omnipotent RF in bacteria, capable of reading all three stop codons.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/genética
Escherichia coli/metabolismo
Mutação
Fatores de Terminação de Peptídeos/genética
Engenharia de Proteínas
[Mh] Termos MeSH secundário: Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Fatores de Terminação de Peptídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Peptide Termination Factors); 0 (prfB protein, E coli)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171230
[Lr] Data última revisão:
171230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785238


  3 / 1503 MEDLINE  
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[PMID]:29023495
[Au] Autor:Loya TJ; O'Rourke TW; Reines D
[Ad] Endereço:Department of Biochemistry, Emory University School of Medicine, Atlanta, GA, United States of America.
[Ti] Título:The hnRNP-like Nab3 termination factor can employ heterologous prion-like domains in place of its own essential low complexity domain.
[So] Source:PLoS One;12(10):e0186187, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many RNA-binding proteins possess domains with a biased amino acid content. A common property of these low complexity domains (LCDs) is that they assemble into an ordered amyloid form, juxtaposing RNA recognition motifs in a subcellular compartment in which RNA metabolism is focused. Yeast Nab3 is one such protein that contains RNA-binding domains and a low complexity, glutamine/proline-rich, prion-like domain that can self-assemble. Nab3 also contains a region of structural homology to human hnRNP-C that resembles a leucine zipper which can oligomerize. Here we show that the LCD and the human hnRNP-C homology domains of Nab3 were experimentally separable, as cells were viable with either segment, but not when both were missing. In exploiting the lethality of deleting these regions of Nab3, we were able to test if heterologous prion-like domains known to assemble into amyloid, could substitute for the native sequence. Those from the hnRNP-like protein Hrp1, the canonical prion Sup35, or the epsin-related protein Ent2, could rescue viability and enable the new Nab3 chimeric protein to support transcription termination. Other low complexity domains from RNA-binding, termination-related proteins or a yeast prion, could not. As well, an unbiased genetic selection revealed a new protein sequence that could rescue the loss of Nab3's essential domain via multimerization. This new sequence and Sup35's prion domain could also rescue the lethal loss of Hrp1's prion-like domain when substituted for it. This suggests there are different cross-functional classes of amyloid-forming LCDs and that appending merely any assembly-competent LCD to Nab3 does not restore function or rescue viability. The analysis has revealed the functional complexity of LCDs and provides a means by which the differing classes of LCD can be dissected and understood.
[Mh] Termos MeSH primário: Proteínas Nucleares/química
Proteínas Nucleares/metabolismo
Fatores de Terminação de Peptídeos/química
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Adaptadoras de Transporte Vesicular/genética
Ribonucleoproteínas Nucleares Heterogêneas Grupo C/química
Seres Humanos
Proteínas Nucleares/genética
Fatores de Terminação de Peptídeos/genética
Domínios Proteicos
Proteínas de Ligação a RNA/genética
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Homologia de Sequência de Aminoácidos
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (ENT2 protein, S cerevisiae); 0 (HNRNPC protein, human); 0 (Heterogeneous-Nuclear Ribonucleoprotein Group C); 0 (NAB3 protein, S cerevisiae); 0 (Nuclear Proteins); 0 (Peptide Termination Factors); 0 (RNA-Binding Proteins); 0 (SUP35 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins)
[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:171013
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186187


  4 / 1503 MEDLINE  
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[PMID]:28910422
[Au] Autor:Wang K; Melki R; Kabani M
[Ad] Endereço:Paris-Saclay Institute of Neuroscience, Centre National de la Recherche Scientifique, Université Paris-Saclay, Gif-sur-Yvette, France.
[Ti] Título:A prolonged chronological lifespan is an unexpected benefit of the [PSI+] prion in yeast.
[So] Source:PLoS One;12(9):e0184905, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Self-replicating 'proteinaceous infectious particles' or prions are responsible for complex heritable traits in the yeast Saccharomyces cerevisiae. Our current understanding of the biology of yeast prions stems from studies mostly done in the context of actively dividing cells in optimal laboratory growth conditions. Evidence suggest that fungal prions exist in the wild where most cells are in a non-dividing quiescent state, because of imperfect growth conditions, scarcity of nutrients and competition. We know little about the faithful transmission of yeast prions in such conditions and their physiological consequences throughout the lifespan of yeast cells. We addressed this issue for the [PSI+] prion that results from the self-assembly of the translation release factor Sup35p into insoluble fibrillar aggregates. [PSI+] leads to increased nonsense suppression and confers phenotypic plasticity in response to environmental fluctuations. Here, we report that while [PSI+] had little to no effect on growth per se, it dramatically improved the survival of yeast cells in stationary phase. Remarkably, prolonged chronological lifespan persisted even after [PSI+] was cured from the cells, suggesting that prions may facilitate the acquisition of complex new traits. Such an important selective advantage may contribute to the evolutionary conservation of the prion-forming ability of Sup35p orthologues in distantly related yeast species.
[Mh] Termos MeSH primário: Adaptação Fisiológica
Fatores de Terminação de Peptídeos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Divisão Celular
Plasticidade Celular
Fenótipo
Príons/metabolismo
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Termination Factors); 0 (Prions); 0 (SUP35 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170915
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184905


  5 / 1503 MEDLINE  
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[PMID]:28827366
[Au] Autor:Maury MM; Chenal-Francisque V; Bracq-Dieye H; Han L; Leclercq A; Vales G; Moura A; Gouin E; Scortti M; Disson O; Vázquez-Boland JA; Lecuit M
[Ad] Endereço:Institut Pasteur, National Reference Centre and WHO Collaborating Centre for Listeria, Paris, France.
[Ti] Título:Spontaneous Loss of Virulence in Natural Populations of Listeria monocytogenes.
[So] Source:Infect Immun;85(11), 2017 Nov.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pathogenesis of depends on the ability of this bacterium to escape from the phagosome of the host cells via the action of the pore-forming toxin listeriolysin O (LLO). Expression of the LLO-encoding gene ( ) requires the transcriptional activator PrfA, and both and genes are essential for virulence. Here, we used the hemolytic activity of LLO as a phenotypic marker to screen for spontaneous virulence-attenuating mutations in Sixty nonhemolytic isolates were identified among a collection of 57,820 confirmed strains isolated from a variety of sources (0.1%). In most cases (56/60; 93.3%), the nonhemolytic phenotype resulted from nonsense, missense, or frameshift mutations in Five strains carried mutations leading to a single amino acid substitution (G299V) or a premature stop codon causing strong virulence attenuation in mice. In one strain, both and (encoding a glutathione synthase required for full PrfA activity) were missing due to genomic rearrangements likely caused by a transposable element. The PrfA/LLO loss-of-function (PrfA /LLO ) mutants belonged to phylogenetically diverse clades of , and most were identified among nonclinical strains (57/60). Consistent with the rare occurrence of loss-of-virulence mutations, we show that and are under purifying selection. Although occurring at a low frequency, PrfA /LLO mutational events in lead to niche restriction and open an evolutionary path for obligate saprophytism in this facultative intracellular pathogen.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Toxinas Bacterianas/genética
Regulação Bacteriana da Expressão Gênica
Proteínas de Choque Térmico/genética
Proteínas Hemolisinas/genética
Listeria monocytogenes/genética
Listeria monocytogenes/patogenicidade
Mutação
Fatores de Terminação de Peptídeos/genética
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Proteínas de Bactérias/metabolismo
Toxinas Bacterianas/metabolismo
Evolução Biológica
Clonagem Molecular
Eritrócitos/microbiologia
Proteínas de Choque Térmico/metabolismo
Proteínas Hemolisinas/metabolismo
Hemólise
Seres Humanos
Listeria monocytogenes/classificação
Listeria monocytogenes/crescimento & desenvolvimento
Listeriose/microbiologia
Listeriose/patologia
Camundongos
Camundongos Endogâmicos BALB C
Fatores de Terminação de Peptídeos/metabolismo
Filogenia
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Seleção Genética
Índice de Gravidade de Doença
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (Heat-Shock Proteins); 0 (Hemolysin Proteins); 0 (Peptide Termination Factors); 0 (PrfA protein, Listeria monocytogenes); 0 (Recombinant Proteins); 72270-41-8 (hlyA protein, Listeria monocytogenes)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE


  6 / 1503 MEDLINE  
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[PMID]:28825483
[Au] Autor:Kumar A; Basu D; Satpati P
[Ad] Endereço:Department of Biosciences and Bioengineering, Indian Institute of Technology, Guwahati , Guwahati 781039, Assam, India.
[Ti] Título:Structure-Based Energetics of Stop Codon Recognition by Eukaryotic Release Factor.
[So] Source:J Chem Inf Model;57(9):2321-2328, 2017 Sep 25.
[Is] ISSN:1549-960X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In translation termination, the eukaryotic release factor (eRF1) recognizes mRNA stop codons (UAA, UAG, or UGA) in a ribosomal A site and triggers release of the nascent polypeptide chain from P-site tRNA. eRF1 is highly selective for U in the first position and a combination of purines (except two consecutive guanines, i.e., GG) in the second and third positions. Eukaryotes decode all three stop codons with a single release factor eRF1, instead of two (RF1 and RF2), in bacteria. Furthermore, unlike bacterial RF1/RF2, eRF1 stabilizes the compact U-turn mRNA configuration in the ribosomal A site by accommodating four nucleotides instead of three. Despite the available cryo-EM structures (resolution ∼3.5-3.8 Å), the energetic principle for eRF1 selectivity toward a stop codon remains a fundamentally unsolved problem. Using cryo-EM structures of eukaryotic translation termination complexes as templates, we carried out molecular dynamics free energy simulations of cognate and near-cognate complexes to quantitatively address the energetics of stop codon recognition by eRF1. Our results suggest that eRF1 has a higher discriminatory power against sense codons, compared to that reported earlier for RF1/RF2. The compact mRNA formed specific intra-mRNA interactions, which itself contributed to stop codon specificity. Furthermore, the specificity is enhanced by the loss of protein-mRNA interactions and, most importantly, by desolvation of the incorrect codons in the near-cognate complexes. Our work provides a clue to how eRF1 discriminates between cognate and near-cognate codons during protein synthesis.
[Mh] Termos MeSH primário: Códon de Terminação/metabolismo
Fatores de Terminação de Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Pareamento de Bases
Códon de Terminação/química
Códon de Terminação/genética
Simulação de Dinâmica Molecular
Fatores de Terminação de Peptídeos/química
Ligação Proteica
Conformação Proteica
Especificidade por Substrato
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Terminator); 0 (Peptide Termination Factors)
[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:170822
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jcim.7b00340


  7 / 1503 MEDLINE  
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[PMID]:28576486
[Au] Autor:Zhang Z; Xu H; Si L; Chen Y; Zhang B; Wang Y; Wu Y; Zhou X; Zhang L; Zhou D
[Ad] Endereço:State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, Beijing 100191, China.
[Ti] Título:Construction of an inducible stable cell line for efficient incorporation of unnatural amino acids in mammalian cells.
[So] Source:Biochem Biophys Res Commun;489(4):490-496, 2017 Aug 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The genetic incorporation of unnatural amino acids (Uaas) with defined properties into proteins at designated sites represents an extremely powerful tool for protein engineering. However, the efficient incorporation of Uaas in response to the amber stop codon in mammalian cells remains a substantial challenge due to the competition from release factor 1(RF1). Addressing this challenge will greatly broaden the power and scope of this technology. Here, we chose the eRF1 mutant, which can selectively enhance Uaa incorporation in response to the amber codon without increasing the readthrough of the opal and ochre codons. Then, we developed an engineered stable cell line using a tetracycline-controlled inducible lentiviral system for the conditional expression of mutant eRF1, which can minimize the potential effect on normal translation termination. Using the eRF1-engineered cells, we provided a 2-fold improvement in the yield of protein containing a Uaa incorporated at a single site, with the protein yield approaching 90% of the wild-type control without the amber codon. Moreover, we achieved the successful incorporation of Uaas at four sites in various proteins at a measured level of 20%.
[Mh] Termos MeSH primário: Aminoácidos/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Células HEK293
Seres Humanos
Fatores de Terminação de Peptídeos/metabolismo
Engenharia de Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (ETF1 protein, human); 0 (Peptide Termination Factors)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170604
[St] Status:MEDLINE


  8 / 1503 MEDLINE  
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[PMID]:28542628
[Au] Autor:Iwakura N; Yokoyama T; Quaglia F; Mitsuoka K; Mio K; Shigematsu H; Shirouzu M; Kaji A; Kaji H
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Thomas Jefferson University, Jefferson Medical College, Philadelphia, Pennsylvania, United States of America.
[Ti] Título:Chemical and structural characterization of a model Post-Termination Complex (PoTC) for the ribosome recycling reaction: Evidence for the release of the mRNA by RRF and EF-G.
[So] Source:PLoS One;12(5):e0177972, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A model Post-Termination Complex (PoTC) used for the discovery of Ribosome Recycling Factor (RRF) was purified and characterized by cryo-electron microscopic analysis and biochemical methods. We established that the model PoTC has mostly one tRNA, at the P/E or P/P position, together with one mRNA. The structural studies were supported by the biochemical measurement of bound tRNA and mRNA. Using this substrate, we establish that the release of tRNA, release of mRNA and splitting of ribosomal subunits occur during the recycling reaction. Order of these events is tRNA release first followed by mRNA release and splitting almost simultaneously. Moreover, we demonstrate that IF3 is not involved in any of the recycling reactions but simply prevents the re-association of split ribosomal subunits. Our finding demonstrates that the important function of RRF includes the release of mRNA, which is often missed by the use of a short ORF with the Shine-Dalgarno sequence near the termination site.
[Mh] Termos MeSH primário: Escherichia coli/genética
Escherichia coli/metabolismo
Terminação Traducional da Cadeia Peptídica/genética
Fator G para Elongação de Peptídeos/metabolismo
Fatores de Terminação de Peptídeos/metabolismo
Proteínas Ribossômicas/metabolismo
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Microscopia Crioeletrônica
Fator de Iniciação 3 em Procariotos/metabolismo
RNA Mensageiro/metabolismo
RNA de Transferência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Elongation Factor G); 0 (Peptide Termination Factors); 0 (Prokaryotic Initiation Factor-3); 0 (RNA, Messenger); 0 (Ribosomal Proteins); 0 (ribosome releasing factor); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177972


  9 / 1503 MEDLINE  
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[PMID]:28537243
[Au] Autor:Bondarev SA; Likholetova DV; Belousov MV; Zhouravleva GA
[Ad] Endereço:Laboratory of Physiological Genetics, Department of Genetics and Biotechnology, St. Petersburg State University, St. Petersburg, 199034 Russia.
[Ti] Título:[Rnq1 protein protects [PSI
[So] Source:Mol Biol (Mosk);51(2):367-371, 2017 Mar-Apr.
[Is] ISSN:0026-8984
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The interaction of [PSI^(+)] and [PIN^(+)] factors in yeast Saccharomyces cerevisiae is known as the first evidence of prions networks. In [PIN^(+)] cells, Rnq1p prion aggregates work as a template for Sup35p aggregation, which is essential for [PSI^(+)] induction. No additional factors are required for subsequent Sup35p aggregation. Nevertheless, several recent reports provide data that indicate a more complex interplay between these prions. Our results show that the presence of Rnq1p in the cell significantly decreases the loss of [PSI^(+)] prion, which is caused by a double mutation in SUP35 (Q61K, Q62K substitutions in the Sup35 protein). These observations support the existence of interaction networks that converge on a strong linkage of prionogenic and prion-like proteins, and the participation of Rnq1 protein in the maintenance of prion [PSI^(+)].
[Mh] Termos MeSH primário: Mutação de Sentido Incorreto
Fatores de Terminação de Peptídeos
Príons
Proteínas de Saccharomyces cerevisiae
Saccharomyces cerevisiae
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Fatores de Terminação de Peptídeos/genética
Fatores de Terminação de Peptídeos/metabolismo
Príons/genética
Príons/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Termination Factors); 0 (Prions); 0 (RNQ1 protein, S cerevisiae); 0 (SUP35 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins)
[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:170525
[St] Status:MEDLINE
[do] DOI:10.7868/S0026898417010050


  10 / 1503 MEDLINE  
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[PMID]:28472342
[Au] Autor:Jamar NH; Kritsiligkou P; Grant CM
[Ad] Endereço:The University of Manchester, Faculty of Biology, Medicine and Health, Manchester M13 9PT, UK.
[Ti] Título:The non-stop decay mRNA surveillance pathway is required for oxidative stress tolerance.
[So] Source:Nucleic Acids Res;45(11):6881-6893, 2017 Jun 20.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Reactive oxygen species (ROS) are toxic by-products of normal aerobic metabolism. ROS can damage mRNAs and the translational apparatus resulting in translational defects and aberrant protein production. Three mRNA quality control systems monitor mRNAs for translational errors: nonsense-mediated decay, non-stop decay (NSD) and no-go decay (NGD) pathways. Here, we show that factors required for the recognition of NSD substrates and components of the SKI complex are required for oxidant tolerance. We found an overlapping requirement for Ski7, which bridges the interaction between the SKI complex and the exosome, and NGD components (Dom34/Hbs1) which have been shown to function in both NSD and NGD. We show that ski7 dom34 and ski7 hbs1 mutants are sensitive to hydrogen peroxide stress and accumulate an NSD substrate. We further show that NSD substrates are generated during ROS exposure as a result of aggregation of the Sup35 translation termination factor, which increases stop codon read-through allowing ribosomes to translate into the 3΄-end of mRNAs. Overexpression of Sup35 decreases stop codon read-through and rescues oxidant tolerance consistent with this model. Our data reveal an unanticipated requirement for the NSD pathway during oxidative stress conditions which prevents the production of aberrant proteins from NSD mRNAs.
[Mh] Termos MeSH primário: Estresse Oxidativo
Estabilidade de RNA
RNA Fúngico/metabolismo
RNA Mensageiro/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Adaptação Fisiológica
Proteínas Adaptadoras de Transdução de Sinal/fisiologia
Proteínas de Ciclo Celular/fisiologia
Endorribonucleases/fisiologia
Proteínas de Ligação ao GTP/fisiologia
Regulação Fúngica da Expressão Gênica
Proteínas de Choque Térmico HSP70/fisiologia
Viabilidade Microbiana
Fatores de Alongamento de Peptídeos/fisiologia
Fatores de Terminação de Peptídeos/genética
Fatores de Terminação de Peptídeos/metabolismo
Biossíntese de Proteínas
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Cell Cycle Proteins); 0 (HBS1 protein, S cerevisiae); 0 (HSP70 Heat-Shock Proteins); 0 (Peptide Elongation Factors); 0 (Peptide Termination Factors); 0 (RNA, Fungal); 0 (RNA, Messenger); 0 (SKI2 protein, S cerevisiae); 0 (SKI7 protein, S cerevisiae); 0 (SUP35 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); EC 3.1.- (Dom34 protein, S cerevisiae); EC 3.1.- (Endoribonucleases); EC 3.6.1.- (GTP-Binding Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx306



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