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Pesquisa : G02.111.660.871.640 [Categoria DeCS]
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  1 / 1825 MEDLINE  
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[PMID]:29342219
[Au] Autor:Hassan MK; Kumar D; Naik M; Dixit M
[Ad] Endereço:School of Biological Sciences, National Institute of Science Education and Research, HBNI, Bhimpur- Padanpur, Jatni, Khurda, Odisha, India.
[Ti] Título:The expression profile and prognostic significance of eukaryotic translation elongation factors in different cancers.
[So] Source:PLoS One;13(1):e0191377, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic translation factors, especially initiation factors have garnered much attention with regards to their role in the onset and progression of different cancers. However, the expression levels and prognostic significance of translation elongation factors remain poorly explored in different cancers. In this study, we have investigated the mRNA transcript levels of seven translation elongation factors in different cancer types using Oncomine and TCGA databases. Furthermore, we have identified the prognostic significance of these factors using Kaplan-Meier Plotter and SurvExpress databases. We observed altered expression levels of all the elongation factors in different cancers. Higher expression of EEF1A2, EEF1B2, EEF1G, EEF1D, EEF1E1 and EEF2 was observed in most of the cancer types, whereas reverse trend was observed for EEF1A1. Overexpression of many factors predicted poor prognosis in breast (EEF1D, EEF1E1, EEF2) and lung cancer (EEF1A2, EEF1B2, EEF1G, EEF1E1). However, we didn't see any common correlation of expression levels of elongation factors with survival outcomes across cancer types. Cancer subtype stratification showed association of survival outcomes and expression levels of elongation factors in specific sub-types of breast, lung and gastric cancer. Most interestingly, we observed a reciprocal relationship between the expression levels of the two EEF1A isoforms viz. EEF1A1 and EEF1A2, in most of the cancer types. Our results suggest that translation elongation factors can have a role in tumorigenesis and affect survival in cancer specific manner. Elongation factors have potential to serve as biomarkers and therapeutic drug targets, yet further study is required. Reciprocal relationship of differential expression between EEF1A isoforms observed in multiple cancer types indicates opposing roles in cancer and needs further investigation.
[Mh] Termos MeSH primário: Neoplasias/genética
Elongação Traducional da Cadeia Peptídica/genética
Transcriptoma/genética
[Mh] Termos MeSH secundário: Transformação Celular Neoplásica
Bases de Dados de Ácidos Nucleicos
Seres Humanos
Estimativa de Kaplan-Meier
Elongação Traducional da Cadeia Peptídica/fisiologia
Fator 1 de Elongação de Peptídeos/genética
Fator 1 de Elongação de Peptídeos/metabolismo
Prognóstico
Biossíntese de Proteínas
Isoformas de Proteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (EEF1A1 protein, human); 0 (EEF1A2 protein, human); 0 (EEF1D protein, human); 0 (Peptide Elongation Factor 1); 0 (Protein Isoforms)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180118
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191377


  2 / 1825 MEDLINE  
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[PMID]:29300771
[Au] Autor:Mateyak MK; Pupek JK; Garino AE; Knapp MC; Colmer SF; Kinzy TG; Dunaway S
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Robert Wood Johnson Medical School, Rutgers, the State University of New Jersey, Piscataway, NJ, United States of America.
[Ti] Título:Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans.
[So] Source:PLoS One;13(1):e0190524, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In most eukaryotic organisms, translation elongation requires two highly conserved elongation factors eEF1A and eEF2. Fungal systems are unique in requiring a third factor, the eukaryotic Elongation Factor 3 (eEF3). For decades, eEF3, a ribosome-dependent ATPase, was considered "fungal-specific", however, recent bioinformatics analysis indicates it may be more widely distributed among other unicellular eukaryotes. In order to determine whether divergent eEF3-like proteins from other eukaryotic organisms can provide the essential functions of eEF3 in budding yeast, the eEF3-like proteins from Schizosaccharomyes pombe and an oomycete, Phytophthora infestans, were cloned and expressed in Saccharomyces cerevisiae. Plasmid shuffling experiments showed that both S. pombe and P. infestans eEF3 can support the growth of S. cerevisiae in the absence of endogenous budding yeast eEF3. Consistent with its ability to provide the essential functions of eEF3, P. infestans eEF3 possessed ribosome-dependent ATPase activity. Yeast cells expressing P. infestans eEF3 displayed reduced protein synthesis due to defects in translation elongation/termination. Identification of eEF3 in divergent species will advance understanding of its function and the ribosome specific determinants that lead to its requirement as well as contribute to the identification of functional domains of eEF3 for potential drug discovery.
[Mh] Termos MeSH primário: Fatores de Alongamento de Peptídeos/metabolismo
Phytophthora infestans/metabolismo
[Mh] Termos MeSH secundário: Elongação Traducional da Cadeia Peptídica
Fatores de Alongamento de Peptídeos/classificação
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptide Elongation Factors)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180105
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190524


  3 / 1825 MEDLINE  
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[PMID]:28977579
[Au] Autor:Belhabich-Baumas K; Joret C; Jády BE; Plisson-Chastang C; Shayan R; Klopp C; Henras AK; Henry Y; Mougin A
[Ad] Endereço:Laboratoire de Biologie Moléculaire Eucaryote, Centre de Biologie Intégrative (CBI), Université de Toulouse, CNRS, UPS, 31000 Toulouse, France.
[Ti] Título:The Rio1p ATPase hinders premature entry into translation of late pre-40S pre-ribosomal particles.
[So] Source:Nucleic Acids Res;45(18):10824-10836, 2017 Oct 13.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytoplasmic maturation of precursors to the small ribosomal subunit in yeast requires the intervention of a dozen assembly factors (AFs), the precise roles of which remain elusive. One of these is Rio1p that seems to intervene at a late step of pre-40S particle maturation. We have investigated the role played by Rio1p in the dynamic association and dissociation of AFs with and from pre-40S particles. Our results indicate that Rio1p depletion leads to the stalling of at least 4 AFs (Nob1p, Tsr1p, Pno1p/Dim2p and Fap7p) in 80S-like particles. We conclude that Rio1p is important for the timely release of these factors from 80S-like particles. In addition, we present immunoprecipitation and electron microscopy evidence suggesting that when Rio1p is depleted, a subset of Nob1p-containing pre-40S particles associate with translating polysomes. Using Nob1p as bait, we purified pre-40S particles from cells lacking Rio1p and performed ribosome profiling experiments which suggest that immature 40S subunits can carry out translation elongation. We conclude that lack of Rio1p allows premature entry of pre-40S particles in the translation process and that the presence of Nob1p and of the 18S rRNA 3' extension in the 20S pre-rRNA is not incompatible with translation elongation.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/fisiologia
Biossíntese de Proteínas
Proteínas Serina-Treonina Quinases/fisiologia
Subunidades Ribossômicas Menores de Eucariotos/metabolismo
Proteínas de Saccharomyces cerevisiae/fisiologia
[Mh] Termos MeSH secundário: Proteínas Nucleares/metabolismo
Elongação Traducional da Cadeia Peptídica
Polirribossomos/metabolismo
Proteínas Ribossômicas/metabolismo
Ribossomos/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (LTV1 protein, S cerevisiae); 0 (NOB1 protein, S cerevisiae); 0 (Nuclear Proteins); 0 (Ribosomal Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (Rio1 protein, S cerevisiae); EC 3.6.1.- (Adenosine Triphosphatases)
[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:171005
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx734


  4 / 1825 MEDLINE  
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[PMID]:28768714
[Au] Autor:Bugaud O; Barbier N; Chommy H; Fiszman N; Le Gall A; Dulin D; Saguy M; Westbrook N; Perronet K; Namy O
[Ad] Endereço:Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91190 Gif sur Yvette, France.
[Ti] Título:Kinetics of CrPV and HCV IRES-mediated eukaryotic translation using single-molecule fluorescence microscopy.
[So] Source:RNA;23(11):1626-1635, 2017 Nov.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein synthesis is a complex multistep process involving many factors that need to interact in a coordinated manner to properly translate the messenger RNA. As translating ribosomes cannot be synchronized over many elongation cycles, single-molecule studies have been introduced to bring a deeper understanding of prokaryotic translation dynamics. Extending this approach to eukaryotic translation is very appealing, but initiation and specific labeling of the ribosomes are much more complicated. Here, we use a noncanonical translation initiation based on internal ribosome entry sites (IRES), and we monitor the passage of individual, unmodified mammalian ribosomes at specific fluorescent milestones along mRNA. We explore initiation by two types of IRES, the intergenic IRES of cricket paralysis virus (CrPV) and the hepatitis C (HCV) IRES, and show that they both strongly limit the rate of the first elongation steps compared to the following ones, suggesting that those first elongation cycles do not correspond to a canonical elongation. This new system opens the possibility of studying both IRES-mediated initiation and elongation kinetics of eukaryotic translation and will undoubtedly be a valuable tool to investigate the role of translation machinery modifications in human diseases.
[Mh] Termos MeSH primário: Dicistroviridae/genética
Dicistroviridae/metabolismo
Hepacivirus/genética
Hepacivirus/metabolismo
Sítios Internos de Entrada Ribossomal
Biossíntese de Proteínas
[Mh] Termos MeSH secundário: Animais
Gryllidae/virologia
Seres Humanos
Técnicas In Vitro
Cinética
Microscopia de Fluorescência
Modelos Biológicos
Elongação Traducional da Cadeia Peptídica
RNA Mensageiro/genética
RNA Viral/genética
Coelhos
Ribossomos/metabolismo
Imagem Individual de Molécula
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Internal Ribosome Entry Sites); 0 (RNA, Messenger); 0 (RNA, Viral)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.1261/rna.061523.117


  5 / 1825 MEDLINE  
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[PMID]:28637336
[Au] Autor:Hayashi N; Sasaki S; Takahashi H; Yamashita Y; Naito S; Onouchi H
[Ad] Endereço:Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan.
[Ti] Título:Identification of Arabidopsis thaliana upstream open reading frames encoding peptide sequences that cause ribosomal arrest.
[So] Source:Nucleic Acids Res;45(15):8844-8858, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Specific sequences of certain nascent peptides cause programmed ribosomal arrest during mRNA translation to control gene expression. In eukaryotes, most known regulatory arrest peptides are encoded by upstream open reading frames (uORFs) present in the 5'-untranslated region of mRNAs. However, to date, a limited number of eukaryotic uORFs encoding arrest peptides have been reported. Here, we searched for arrest peptide-encoding uORFs among Arabidopsis thaliana uORFs with evolutionarily conserved peptide sequences. Analysis of in vitro translation products of 22 conserved uORFs identified three novel uORFs causing ribosomal arrest in a peptide sequence-dependent manner. Stop codon-scanning mutagenesis, in which the effect of changing the uORF stop codon position on the ribosomal arrest was examined, and toeprint analysis revealed that two of the three uORFs cause ribosomal arrest during translation elongation, whereas the other one causes ribosomal arrest during translation termination. Transient expression assays showed that the newly identified arrest-causing uORFs exerted a strong sequence-dependent repressive effect on the expression of the downstream reporter gene in A. thaliana protoplasts. These results suggest that the peptide sequences of the three uORFs identified in this study cause ribosomal arrest in the uORFs, thereby repressing the expression of proteins encoded by the main ORFs.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Regulação da Expressão Gênica de Plantas
Fases de Leitura Aberta
Elongação Traducional da Cadeia Peptídica
Terminação Traducional da Cadeia Peptídica
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Sequência de Aminoácidos
Arabidopsis/metabolismo
Proteínas de Arabidopsis/metabolismo
Códon de Terminação
Sequência Conservada
Genes Reporter
Luciferases/genética
Luciferases/metabolismo
Protoplastos/metabolismo
Ribossomos/genética
Ribossomos/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (Arabidopsis Proteins); 0 (Codon, Terminator); EC 1.13.12.- (Luciferases)
[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:170623
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx528


  6 / 1825 MEDLINE  
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[PMID]:28598992
[Au] Autor:Rogers DW; Böttcher MA; Traulsen A; Greig D
[Ad] Endereço:Experimental Evolution Research Group, Max Planck Institute for Evolutionary Biology, Plön, Germany.
[Ti] Título:Ribosome reinitiation can explain length-dependent translation of messenger RNA.
[So] Source:PLoS Comput Biol;13(6):e1005592, 2017 Jun.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Models of mRNA translation usually presume that transcripts are linear; upon reaching the end of a transcript each terminating ribosome returns to the cytoplasmic pool before initiating anew on a different transcript. A consequence of linear models is that faster translation of a given mRNA is unlikely to generate more of the encoded protein, particularly at low ribosome availability. Recent evidence indicates that eukaryotic mRNAs are circularized, potentially allowing terminating ribosomes to preferentially reinitiate on the same transcript. Here we model the effect of ribosome reinitiation on translation and show that, at high levels of reinitiation, protein synthesis rates are dominated by the time required to translate a given transcript. Our model provides a simple mechanistic explanation for many previously enigmatic features of eukaryotic translation, including the negative correlation of both ribosome densities and protein abundance on transcript length, the importance of codon usage in determining protein synthesis rates, and the negative correlation between transcript length and both codon adaptation and 5' mRNA folding energies. In contrast to linear models where translation is largely limited by initiation rates, our model reveals that all three stages of translation-initiation, elongation, and termination/reinitiation-determine protein synthesis rates even at low ribosome availability.
[Mh] Termos MeSH primário: Iniciação Traducional da Cadeia Peptídica/genética
Modificação Traducional de Proteínas/genética
RNA Mensageiro/química
RNA Mensageiro/genética
Ribossomos/química
Ribossomos/genética
[Mh] Termos MeSH secundário: Simulação por Computador
Modelos Químicos
Modelos Genéticos
Elongação Traducional da Cadeia Peptídica/genética
RNA Mensageiro/ultraestrutura
Ribossomos/ultraestrutura
Relação Estrutura-Atividade
Fatores de Transcrição/química
Fatores de Transcrição/genética
Fatores de Transcrição/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Transcription Factors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005592


  7 / 1825 MEDLINE  
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[PMID]:28582582
[Au] Autor:Zhao F; Yu CH; Liu Y
[Ad] Endereço:Department of Physiology, The University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
[Ti] Título:Codon usage regulates protein structure and function by affecting translation elongation speed in Drosophila cells.
[So] Source:Nucleic Acids Res;45(14):8484-8492, 2017 Aug 21.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Codon usage biases are found in all eukaryotic and prokaryotic genomes and have been proposed to regulate different aspects of translation process. Codon optimality has been shown to regulate translation elongation speed in fungal systems, but its effect on translation elongation speed in animal systems is not clear. In this study, we used a Drosophila cell-free translation system to directly compare the velocity of mRNA translation elongation. Our results demonstrate that optimal synonymous codons speed up translation elongation while non-optimal codons slow down translation. In addition, codon usage regulates ribosome movement and stalling on mRNA during translation. Finally, we show that codon usage affects protein structure and function in vitro and in Drosophila cells. Together, these results suggest that the effect of codon usage on translation elongation speed is a conserved mechanism from fungi to animals that can affect protein folding in eukaryotic organisms.
[Mh] Termos MeSH primário: Códon/genética
Proteínas de Drosophila/genética
Elongação Traducional da Cadeia Peptídica/genética
Biossíntese de Proteínas/genética
[Mh] Termos MeSH secundário: Animais
Western Blotting
Linhagem Celular
Sistema Livre de Células
Proteínas de Drosophila/química
Proteínas de Drosophila/metabolismo
Drosophila melanogaster/citologia
Drosophila melanogaster/genética
Drosophila melanogaster/metabolismo
Dobramento de Proteína
Estabilidade de RNA/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Ribossomos/genética
Ribossomos/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (Drosophila Proteins); 0 (RNA, Messenger)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx501


  8 / 1825 MEDLINE  
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[PMID]:28549188
[Au] Autor:Pelechano V; Alepuz P
[Ad] Endereço:SciLifeLab, Department of Microbiology, Tumor and Cell Biology. Karolinska Institutet, P-Box 1031. 171 21 Solna, Sweden.
[Ti] Título:eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences.
[So] Source:Nucleic Acids Res;45(12):7326-7338, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:eIF5A is an essential protein involved in protein synthesis, cell proliferation and animal development. High eIF5A expression is observed in many tumor types and has been linked to cancer metastasis. Recent studies have shown that eIF5A facilitates the translation elongation of stretches of consecutive prolines. Activated eIF5A binds to the empty E-site of stalled ribosomes, where it is thought to interact with the peptidyl-tRNA situated at the P-site. Here, we report a genome-wide analysis of ribosome stalling in Saccharomyces cerevisiae eIF5A depleted cells using 5Pseq. We confirm that, in the absence of eIF5A, ribosomes stall at proline stretches, and extend previous studies by identifying eIF5A-dependent ribosome pauses at termination and at >200 tripeptide motifs. We show that presence of proline, glycine and charged amino acids at the peptidyl transferase center and at the beginning of the peptide exit tunnel arrest ribosomes in eIF5A-depleted cells. Lack of eIF5A also renders ribosome accumulation at the stop codons. Our data indicate specific protein functional groups under the control of eIF5A, including ER-coupled translation and GTPases in yeast and cytoskeleton organization, collagen metabolism and cell differentiation in humans. Our results support a broad mRNA-specific role of eIF5A in translation and identify the conserved motifs that affect translation elongation from yeast to humans.
[Mh] Termos MeSH primário: Genoma Fúngico
Elongação Traducional da Cadeia Peptídica
Fatores de Iniciação de Peptídeos/genética
Proteínas de Ligação a RNA/genética
Ribossomos/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sítios de Ligação
GTP Fosfo-Hidrolases/genética
GTP Fosfo-Hidrolases/metabolismo
Regulação Fúngica da Expressão Gênica
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Fatores de Iniciação de Peptídeos/metabolismo
Prolina/metabolismo
Ligação Proteica
Proteínas de Ligação a RNA/metabolismo
Ribossomos/metabolismo
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Initiation Factors); 0 (RNA-Binding Proteins); 0 (eukaryotic translation initiation factor 5A); 9DLQ4CIU6V (Proline); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx479


  9 / 1825 MEDLINE  
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[PMID]:28483649
[Au] Autor:Po P; Delaney E; Gamper H; Szantai-Kis DM; Speight L; Tu L; Kosolapov A; Petersson EJ; Hou YM; Deutsch C
[Ad] Endereço:Department of Physiology, University of Pennsylvania, Philadelphia, PA 19104, USA.
[Ti] Título:Effect of Nascent Peptide Steric Bulk on Elongation Kinetics in the Ribosome Exit Tunnel.
[So] Source:J Mol Biol;429(12):1873-1888, 2017 Jun 16.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:All proteins are synthesized by the ribosome, a macromolecular complex that accomplishes the life-sustaining tasks of faithfully decoding mRNA and catalyzing peptide bond formation at the peptidyl transferase center (PTC). The ribosome has evolved an exit tunnel to host the elongating new peptide, protect it from proteolytic digestion, and guide its emergence. It is here that the nascent chain begins to fold. This folding process depends on the rate of translation at the PTC. We report here that besides PTC events, translation kinetics depend on steric constraints on nascent peptide side chains and that confined movements of cramped side chains within and through the tunnel fine-tune elongation rates.
[Mh] Termos MeSH primário: Elongação Traducional da Cadeia Peptídica
Proteínas/química
Proteínas/metabolismo
Ribossomos/química
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Cinética
Modelos Biológicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170510
[St] Status:MEDLINE


  10 / 1825 MEDLINE  
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[PMID]:28480640
[Au] Autor:Prabhakar A; Choi J; Wang J; Petrov A; Puglisi JD
[Ad] Endereço:Department of Structural Biology, Stanford University School of Medicine, Stanford, California, 94305.
[Ti] Título:Dynamic basis of fidelity and speed in translation: Coordinated multistep mechanisms of elongation and termination.
[So] Source:Protein Sci;26(7):1352-1362, 2017 Jul.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:As the universal machine that transfers genetic information from RNA to protein, the ribosome synthesizes proteins with remarkably high fidelity and speed. This is a result of the accurate and efficient decoding of mRNA codons via multistep mechanisms during elongation and termination stages of translation. These mechanisms control how the correct sense codon is recognized by a tRNA for peptide elongation, how the next codon is presented to the decoding center without change of frame during translocation, and how the stop codon is discriminated for timely release of the nascent peptide. These processes occur efficiently through coupling of chemical energy expenditure, ligand interactions, and conformational changes. Understanding this coupling in detail required integration of many techniques that were developed in the past two decades. This multidisciplinary approach has revealed the dynamic nature of translational control and uncovered how external cellular factors such as tRNA abundance and mRNA modifications affect the synthesis of the protein product. Insights from these studies will aid synthetic biology and therapeutic approaches to translation.
[Mh] Termos MeSH primário: Códon de Terminação/metabolismo
Elongação Traducional da Cadeia Peptídica/fisiologia
Terminação Traducional da Cadeia Peptídica/fisiologia
RNA de Transferência/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Codon, Terminator); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3190



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