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  1 / 221 MEDLINE  
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[PMID]:28655767
[Au] Autor:Xu L; Liu X; Sheng N; Oo KS; Liang J; Chionh YH; Xu J; Ye F; Gao YG; Dedon PC; Fu XY
[Ad] Endereço:From the Cancer Science Institute of Singapore, National University of Singapore, 14 Medical Drive, 117599 Singapore.
[Ti] Título:Three distinct 3-methylcytidine (m C) methyltransferases modify tRNA and mRNA in mice and humans.
[So] Source:J Biol Chem;292(35):14695-14703, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chemical RNA modifications are central features of epitranscriptomics, highlighted by the discovery of modified ribonucleosides in mRNA and exemplified by the critical roles of RNA modifications in normal physiology and disease. Despite a resurgent interest in these modifications, the biochemistry of 3-methylcytidine (m C) formation in mammalian RNAs is still poorly understood. However, the recent discovery of as the second gene responsible for m C presence in RNA in fission yeast raises the possibility that multiple enzymes are involved in m C formation in mammals as well. Here, we report the discovery and characterization of three distinct m C-contributing enzymes in mice and humans. We found that methyltransferase-like (METTL) 2 and 6 contribute m C in specific tRNAs and that METTL8 only contributes m C to mRNA. MS analysis revealed that there is an ∼30-40% and ∼10-15% reduction, respectively, in and null-mutant cells, of m C in total tRNA, and primer extension analysis located METTL2-modified m C at position 32 of tRNA isoacceptors and tRNA We also noted that METTL6 interacts with seryl-tRNA synthetase in an RNA-dependent manner, suggesting a role for METTL6 in modifying serine tRNA isoacceptors. , however, modified only mRNA, as determined by biochemical and genetic analyses in null-mutant mice and two human mutant cell lines. Our findings provide the first evidence of the existence of m C modification in mRNA, and the discovery of METTL8 as an mRNA m C writer enzyme opens the door to future studies of other m C epitranscriptomic reader and eraser functions.
[Mh] Termos MeSH primário: Citidina/análogos & derivados
Fígado/metabolismo
Metiltransferases/metabolismo
Processamento Pós-Transcricional do RNA
RNA Mensageiro/metabolismo
RNA de Transferência/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Citidina/metabolismo
Seres Humanos
Isoenzimas/genética
Isoenzimas/metabolismo
Fígado/enzimologia
Metilação
Metiltransferases/antagonistas & inibidores
Metiltransferases/química
Metiltransferases/genética
Camundongos
Camundongos Knockout
Camundongos Mutantes
Mutação
Interferência de RNA
RNA de Transferência de Arginina/metabolismo
RNA de Transferência de Serina/metabolismo
RNA de Transferência de Treonina/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Serina-tRNA Ligase/química
Serina-tRNA Ligase/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 0 (RNA, Messenger); 0 (RNA, Transfer, Arg); 0 (RNA, Transfer, Ser); 0 (RNA, Transfer, Thr); 0 (Recombinant Fusion Proteins); 2140-64-9 (3-methylcytidine); 5CSZ8459RP (Cytidine); 9014-25-9 (RNA, Transfer); EC 2.1.1.- (Methyltransferases); EC 6.1.1.11 (Serine-tRNA Ligase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.798298


  2 / 221 MEDLINE  
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[PMID]:28331090
[Au] Autor:Peterlin BM; Liu P; Wang X; Cary D; Shao W; Leoz M; Hong T; Pan T; Fujinaga K
[Ad] Endereço:Departments of Medicine, Microbiology and Immunology, University of California, San Francisco, San Francisco, California, USA.
[Ti] Título:Hili Inhibits HIV Replication in Activated T Cells.
[So] Source:J Virol;91(11), 2017 Jun 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:P-element-induced wimpy-like (Piwil) proteins restrict the replication of mobile genetic elements in the germ line. They are also expressed in many transformed cell lines. In this study, we discovered that the human Piwil 2 (Hili) protein can also inhibit HIV replication, especially in activated CD4 T cells that are the preferred target cells for this virus in the infected host. Although resting cells did not express Hili, its expression was rapidly induced following T cell activation. In these cells and transformed cell lines, depletion of Hili increased levels of viral proteins and new viral particles. Further studies revealed that Hili binds to tRNA. Some of the tRNAs represent rare tRNA species, whose codons are overrepresented in the viral genome. Targeting tRNA (UCU) with an antisense oligonucleotide replicated effects of Hili and also inhibited HIV replication. Finally, Hili also inhibited the retrotransposition of the endogenous intracysternal A particle (IAP) by a similar mechanism. Thus, Hili joins a list of host proteins that inhibit the replication of HIV and other mobile genetic elements. Piwil proteins inhibit the movement of mobile genetic elements in the germ line. In their absence, sperm does not form and male mice are sterile. This inhibition is thought to occur via small Piwi-interacting RNAs (piRNAs). However, in some species and in human somatic cells, Piwil proteins bind primarily to tRNA. In this report, we demonstrate that human Piwil proteins, especially Hili, not only bind to select tRNA species, including rare tRNAs, but also inhibit HIV replication. Importantly, T cell activation induces the expression of Hili in CD4 T cells. Since Hili also inhibited the movement of an endogenous retrovirus (IAP), our finding shed new light on this intracellular resistance to exogenous and endogenous retroviruses as well as other mobile genetic elements.
[Mh] Termos MeSH primário: Proteínas Argonauta/metabolismo
HIV-1/fisiologia
Ativação Linfocitária
Replicação Viral
[Mh] Termos MeSH secundário: Proteínas Argonauta/deficiência
Proteínas Argonauta/genética
Proteínas Argonauta/imunologia
Linhagem Celular
Retrovirus Endógenos/metabolismo
Células HEK293
HIV-1/genética
Células HeLa
Seres Humanos
Oligonucleotídeos Antissenso/genética
Ligação Proteica
RNA Interferente Pequeno/metabolismo
RNA de Transferência/metabolismo
RNA de Transferência de Arginina/genética
RNA de Transferência de Arginina/metabolismo
Linfócitos T/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Argonaute Proteins); 0 (Oligonucleotides, Antisense); 0 (PIWIL2 protein, human); 0 (RNA, Small Interfering); 0 (RNA, Transfer, Arg); 9014-25-9 (RNA, Transfer)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171112
[Lr] Data última revisão:
171112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170324
[St] Status:MEDLINE


  3 / 221 MEDLINE  
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[PMID]:27502052
[Au] Autor:Jain V; Yogavel M; Sharma A
[Ad] Endereço:Molecular Medicine Group, International Centre for Genetic Engineering and Biotechnology (ICGEB), Aruna Asaf Ali Road, New Delhi 110067, India.
[Ti] Título:Dimerization of Arginyl-tRNA Synthetase by Free Heme Drives Its Inactivation in Plasmodium falciparum.
[So] Source:Structure;24(9):1476-87, 2016 Sep 06.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Excess cellular heme is toxic, and malaria parasites regulate its levels during hemoglobin digestion. Aminoacyl-tRNA synthetases are ubiquitous enzymes, and of these, arginyl-tRNA synthetase (RRS) is unique as its enzymatic product of charged tRNA is required for protein synthesis and degradation. We show that Plasmodium falciparum arginyl-tRNA synthetase (PfRRS) is an active, cytosolic, and monomeric enzyme. Its high-resolution crystal structure highlights critical structural differences with the human enzyme. We further show that hemin binds to and inhibits the aminoacylation activity of PfRRS. Hemin induces a dimeric form of PfRRS that is thus rendered enzymatically dead as it is unable to recognize its cognate tRNA(arg). Excessive hemin in chloroquine-treated malaria parasites results in significantly reduced charged tRNA(arg) levels, thus suggesting deceleration of protein synthesis. These data together suggest that the inhibition of Plasmodium falciparum arginyl-tRNA synthetase can now be synergized with existing antimalarials for more potent drug cocktails against malaria parasites.
[Mh] Termos MeSH primário: Arginina-tRNA Ligase/química
Arginina/química
Heme/química
Hemina/química
Plasmodium falciparum/efeitos dos fármacos
Proteínas de Protozoários/química
RNA de Transferência de Arginina/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antimaláricos/química
Antimaláricos/farmacologia
Arginina/metabolismo
Arginina-tRNA Ligase/genética
Arginina-tRNA Ligase/metabolismo
Sítios de Ligação
Cloroquina/química
Cloroquina/farmacologia
Cristalografia por Raios X
Expressão Gênica
Heme/farmacologia
Hemina/farmacologia
Seres Humanos
Modelos Moleculares
Plasmodium falciparum/enzimologia
Plasmodium falciparum/genética
Plasmodium falciparum/crescimento & desenvolvimento
Ligação Proteica
Biossíntese de Proteínas/efeitos dos fármacos
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estrutura Secundária de Proteína
Proteínas de Protozoários/genética
Proteínas de Protozoários/metabolismo
RNA de Transferência de Arginina/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade da Espécie
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimalarials); 0 (Protozoan Proteins); 0 (RNA, Transfer, Arg); 0 (Recombinant Proteins); 42VZT0U6YR (Heme); 743LRP9S7N (Hemin); 886U3H6UFF (Chloroquine); 94ZLA3W45F (Arginine); EC 6.1.1.19 (Arginine-tRNA Ligase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE


  4 / 221 MEDLINE  
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[PMID]:27174972
[Au] Autor:He X; Liu L
[Ad] Endereço:The State Key Laboratory of Biocontrol, School of Life Sciences, Sun Yat-sen University, Guangzhou 510275, China. hexiongl@mail.sysu.edu.cn liul47@mail.sysu.edu.cn.
[Ti] Título:EVOLUTION. Toward a prospective molecular evolution.
[So] Source:Science;352(6287):769-70, 2016 May 13.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Epistasia Genética
Regulação Fúngica da Expressão Gênica
Genes Fúngicos
Aptidão Genética
Dobramento de RNA
RNA Nucleolar Pequeno/genética
RNA de Transferência de Arginina/química
RNA de Transferência de Arginina/genética
Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:COMMENT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Small Nucleolar); 0 (RNA, Transfer, Arg)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:160513
[Lr] Data última revisão:
160513
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160514
[St] Status:MEDLINE
[do] DOI:10.1126/science.aaf7543


  5 / 221 MEDLINE  
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[PMID]:27151886
[Au] Autor:Lee KB; Hou CY; Kim CE; Kim DM; Suga H; Kang TJ
[Ad] Endereço:Department of Chemical and Biochemical Engineering, Dongguk University-Seoul, Seoul, 100-715, South Korea.
[Ti] Título:Genetic Code Expansion by Degeneracy Reprogramming of Arginyl Codons.
[So] Source:Chembiochem;17(13):1198-201, 2016 07 01.
[Is] ISSN:1439-7633
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The genetic code in most organisms codes for 20 proteinogenic amino acids or translation stop. In order to encode more than 20 amino acids in the coding system, one of stop codons is usually reprogrammed to encode a non-proteinogenic amino acid. Although this approach works, usually only one amino acid is added to the amino acid repertoire. In this study, we incorporated non-proteinogenic amino acids into a protein by using a sense codon. As all the codons are allocated in the universal genetic code, we destroyed all the tRNA(Arg) in a cell-free protein synthesis system by using a tRNA(Arg) -specific tRNase, colicin D. Then by supplementing the system with tRNACCU , the translation system was partially restored. Through this creative destruction, reprogrammable codons were successfully created in the system to encode modified lysines along with the 20 proteinogenic amino acids.
[Mh] Termos MeSH primário: Arginina/genética
Evolução Molecular Direcionada
Código Genético
[Mh] Termos MeSH secundário: Códon
Colicinas/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas de Fluorescência Verde/biossíntese
Proteínas de Fluorescência Verde/genética
Biossíntese de Proteínas/genética
RNA de Transferência de Arginina/genética
RNA de Transferência de Arginina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Codon); 0 (Colicins); 0 (RNA, Transfer, Arg); 0 (enhanced green fluorescent protein); 147336-22-9 (Green Fluorescent Proteins); 94ZLA3W45F (Arginine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160507
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201600111


  6 / 221 MEDLINE  
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[PMID]:27085088
[Au] Autor:Ishimura R; Nagy G; Dotu I; Chuang JH; Ackerman SL
[Ad] Endereço:Howard Hughes Medical Institute, The Jackson Laboratory for Mammalian Genetics, Bar Harbor, United States.
[Ti] Título:Activation of GCN2 kinase by ribosome stalling links translation elongation with translation initiation.
[So] Source:Elife;5, 2016 Apr 16.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ribosome stalling during translation has recently been shown to cause neurodegeneration, yet the signaling pathways triggered by stalled elongation complexes are unknown. To investigate these pathways we analyzed the brain of C57BL/6J-Gtpbp2(nmf205)(-/-) mice in which neuronal elongation complexes are stalled at AGA codons due to deficiencies in a tRNA(Arg)UCU tRNA and GTPBP2, a mammalian ribosome rescue factor. Increased levels of phosphorylation of eIF2α (Ser51) were detected prior to neurodegeneration in these mice and transcriptome analysis demonstrated activation of ATF4, a key transcription factor in the integrated stress response (ISR) pathway. Genetic experiments showed that this pathway was activated by the eIF2α kinase, GCN2, in an apparent deacylated tRNA-independent fashion. Further we found that the ISR attenuates neurodegeneration in C57BL/6J-Gtpbp2(nmf205)(-/-) mice, underscoring the importance of cellular and stress context on the outcome of activation of this pathway. These results demonstrate the critical interplay between translation elongation and initiation in regulating neuron survival during cellular stress.
[Mh] Termos MeSH primário: Elongação Traducional da Cadeia Peptídica
Iniciação Traducional da Cadeia Peptídica
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Ribossomos/metabolismo
[Mh] Termos MeSH secundário: Fator 4 Ativador da Transcrição/biossíntese
Animais
Fator de Iniciação 2 em Eucariotos/metabolismo
Proteínas de Ligação ao GTP/deficiência
Perfilação da Expressão Gênica
Camundongos Endogâmicos C57BL
Neurônios/fisiologia
Fosforilação
Processamento de Proteína Pós-Traducional
RNA de Transferência de Arginina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Atf4 protein, mouse); 0 (Eukaryotic Initiation Factor-2); 0 (RNA, Transfer, Arg); 145891-90-3 (Activating Transcription Factor 4); EC 2.7.11.1 (Eif2ak4 protein, mouse); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.6.1.- (GTP-Binding Proteins); EC 3.6.1.- (GTPBP2 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160417
[St] Status:MEDLINE


  7 / 221 MEDLINE  
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[PMID]:27080104
[Au] Autor:Li C; Qian W; Maclean CJ; Zhang J
[Ad] Endereço:Department of Ecology and Evolutionary Biology, University of Michigan, Ann Arbor, MI 48109, USA.
[Ti] Título:The fitness landscape of a tRNA gene.
[So] Source:Science;352(6287):837-40, 2016 May 13.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fitness landscapes describe the genotype-fitness relationship and represent major determinants of evolutionary trajectories. However, the vast genotype space, coupled with the difficulty of measuring fitness, has hindered the empirical determination of fitness landscapes. Combining precise gene replacement and next-generation sequencing, we quantified Darwinian fitness under a high-temperature challenge for more than 65,000 yeast strains, each carrying a unique variant of the single-copy tRNA(CCU)(Arg) gene at its native genomic location. Approximately 1% of single point mutations in the gene were beneficial and 42% were deleterious. Almost half of all mutation pairs exhibited statistically significant epistasis, which had a strong negative bias, except when the mutations occurred at Watson-Crick paired sites. Fitness was broadly correlated with the predicted fraction of correctly folded transfer RNA (tRNA) molecules, thereby revealing a biophysical basis of the fitness landscape.
[Mh] Termos MeSH primário: Genes Fúngicos
Aptidão Genética
Dobramento de RNA
RNA de Transferência de Arginina/química
RNA de Transferência de Arginina/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Anticódon/química
Anticódon/genética
Pareamento de Bases
Análise Mutacional de DNA
Epistasia Genética
Evolução Molecular
Dosagem de Genes
Regulação Fúngica da Expressão Gênica
Temperatura Alta
Mutação Puntual
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Anticodon); 0 (RNA, Transfer, Arg)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160416
[St] Status:MEDLINE
[do] DOI:10.1126/science.aae0568


  8 / 221 MEDLINE  
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[PMID]:27029281
[Au] Autor:Igloi GL; Aldinger CA
[Ad] Endereço:Institut für Biologie III, Universität Freiburg, Freiburg, Germany.
[Ti] Título:Where have all the inosines gone? Conflicting evidence for A-to-I editing of the anticodon of higher eukaryotic tRNAACGArg questions the dogma of a universal wobble-mediated decoding of CGN codons.
[So] Source:IUBMB Life;68(6):419-22, 2016 Jun.
[Is] ISSN:1521-6551
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Codon-anticodon recognition between triplets of an mRNA and a specific tRNA is the key element in the translation of the genetic code. In general, the precision of this process is dominated by a strict Watson-Crick base-pairing scheme. However, the degeneracy of the genetic code led Crick to propose the Wobble Hypothesis, permitting a less restraining interaction with the third base of the codon and involving the participation of inosine for decoding C-ending codons. The concept that the anticodon base A34 of tRNAACGArg in all eukaryotes, eubacteria, and plant chloroplasts is converted to I34 is firmly anchored in the literature despite conflicting evidence for its existence in higher eukaryote cytoplasmic tRNAACGArg. Here, we provide additional data and summarize the arguments favoring and contradicting post-transcriptional deamination of this position. A hypothesis that resolves the apparent conflict is proposed. © 2016 IUBMB Life, 68(6):419-422, 2016.
[Mh] Termos MeSH primário: Anticódon
Códon
Inosina/genética
Edição de RNA
RNA de Transferência de Arginina/metabolismo
[Mh] Termos MeSH secundário: Adenosina/metabolismo
Citoplasma/genética
Citoplasma/metabolismo
Células Eucarióticas
Código Genético
Seres Humanos
Inosina/metabolismo
RNA de Transferência de Arginina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticodon); 0 (Codon); 0 (RNA, Transfer, Arg); 5A614L51CT (Inosine); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE
[do] DOI:10.1002/iub.1497


  9 / 221 MEDLINE  
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[PMID]:26844776
[Au] Autor:McShane A; Hok E; Tomberlin J; Eriani G; Geslain R
[Ad] Endereço:Laboratory of tRNA biology, Department of Biology, College of Charleston, Charleston, South Carolina, United States of America.
[Ti] Título:The Enzymatic Paradox of Yeast Arginyl-tRNA Synthetase: Exclusive Arginine Transfer Controlled by a Flexible Mechanism of tRNA Recognition.
[So] Source:PLoS One;11(2):e0148460, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Identity determinants are essential for the accurate recognition of transfer RNAs by aminoacyl-tRNA synthetases. To date, arginine determinants in the yeast Saccharomyces cerevisiae have been identified exclusively in vitro and only on a limited number of tRNA Arginine isoacceptors. In the current study, we favor a full cellular approach and expand the investigation of arginine determinants to all four tRNA Arg isoacceptors. More precisely, this work scrutinizes the relevance of the tRNA nucleotides at position 20, 35 and 36 in the yeast arginylation reaction. We built 21 mutants by site-directed mutagenesis and tested their functionality in YAL5, a previously engineered yeast knockout deficient for the expression of tRNA Arg CCG. Arginylation levels were also monitored using Northern blot. Our data collected in vivo correlate with previous observations. C35 is the prominent arginine determinant followed by G36 or U36 (G/U36). In addition, although there is no major arginine determinant in the D loop, the recognition of tRNA Arg ICG relies to some extent on the nucleotide at position 20. This work refines the existing model for tRNA Arg recognition. Our observations indicate that yeast Arginyl-tRNA synthetase (yArgRS) relies on distinct mechanisms to aminoacylate the four isoacceptors. Finally, according to our refined model, yArgRS is able to accommodate tRNA Arg scaffolds presenting N34, C/G35 and G/A/U36 anticodons while maintaining specificity. We discuss the mechanistic and potential physiological implications of these findings.
[Mh] Termos MeSH primário: Arginina-tRNA Ligase/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Anticódon
Arginina/metabolismo
Mutação
Fenótipo
Ligação Proteica
RNA de Transferência/genética
RNA de Transferência/metabolismo
RNA de Transferência de Arginina/genética
RNA de Transferência de Arginina/metabolismo
Saccharomyces cerevisiae/genética
Especificidade por Substrato
Aminoacilação de RNA de Transferência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anticodon); 0 (RNA, Transfer, Arg); 9014-25-9 (RNA, Transfer); 94ZLA3W45F (Arginine); EC 6.1.1.19 (Arginine-tRNA Ligase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160205
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0148460


  10 / 221 MEDLINE  
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[PMID]:24983150
[Au] Autor:Luo Z
[Ad] Endereço:a Department of the Emergency Center , The First Affiliated Hospital of Zhengzhou University , Zhengzhou , China.
[Ti] Título:Mitochondrial tRNAArg T10454C variant may not influence the clinical expression of deafness associated 12S rRNA A1555G mutation.
[So] Source:Mitochondrial DNA A DNA Mapp Seq Anal;27(2):1137-40, 2016.
[Is] ISSN:2470-1408
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In this study, we examined the "pathogenic" role of the T10454C mutation in mitochondrial tRNA(Arg) gene in deafness expression as increasing reports provided an active role of this mutation in clinical manifestation of deafness associated 12S rRNA A1555G mutation. For this purpose, we reanalyzed the complete mitochondrial DNA (mtDNA) sequence data containing the T10454C mutation. Moreover, we analyzed the reported "polymorphisms" of mtDNA in the proband using the phylogentic approach. To our surprise, other mutations which occurred at protein-coding genes played more important roles in resulting mitochondrial dysfunctions by using the bioinformatic tool. In addition, evolutionary conservation analysis of the T10454C mutation indicated that this mutation was not conserved between different species. To our knowledge, this is the first report that the T10454C variant may not modulate the phenotypic expression of the deafness associated A1555G mutation.
[Mh] Termos MeSH primário: Surdez
Regulação da Expressão Gênica
Mutação Puntual
RNA Ribossômico
RNA de Transferência de Arginina
RNA
[Mh] Termos MeSH secundário: Linhagem Celular
Surdez/genética
Surdez/metabolismo
Seres Humanos
RNA/genética
RNA/metabolismo
RNA Ribossômico/biossíntese
RNA Ribossômico/genética
RNA de Transferência de Arginina/genética
RNA de Transferência de Arginina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Ribosomal); 0 (RNA, Transfer, Arg); 0 (RNA, mitochondrial); 0 (RNA, ribosomal, 12S); 63231-63-0 (RNA)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140702
[St] Status:MEDLINE
[do] DOI:10.3109/19401736.2014.933337



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