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[PMID]:29223159
[Au] Autor:Baleva MV; Meyer M; Entelis N; Tarassov I; Kamenski P; Masquida B
[Ad] Endereço:GMGM, CNRS - University of Strasbourg, UMR 7156, Strasbourg, 67081, France. b.masquida@unistra.fr.
[Ti] Título:Factors beyond Enolase 2 and Mitochondrial Lysyl-tRNA Synthetase Precursor Are Required for tRNA Import into Yeast Mitochondria.
[So] Source:Biochemistry (Mosc);82(11):1324-1335, 2017 Nov.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In yeast, the import of tRNA with CUU anticodon (tRK1) relies on a complex mechanism where interaction with enolase 2 (Eno2p) dictates a deep conformational change of the tRNA. This event is believed to mask the tRNA from the cytosolic translational machinery to re-direct it towards the mitochondria. Once near the mitochondrial outer membrane, the precursor of the mitochondrial lysyl-tRNA synthetase (preMsk1p) takes over enolase to carry the tRNA within the mitochondrial matrix, where it is supposed to participate in translation following correct refolding. Biochemical data presented in this report focus on the role of enolase. They show that despite the inability of Eno2p alone to form a complex with tRK1, mitochondrial import can be recapitulated in vitro using fractions of yeast extracts sharing either recombinant or endogenous yeast Eno2p as one of the main components. Taken together, our data suggest the existence of a protein complex containing Eno2p that is involved in RNA mitochondrial import.
[Mh] Termos MeSH primário: Lisina-tRNA Ligase/fisiologia
Mitocôndrias/metabolismo
Fosfopiruvato Hidratase/fisiologia
RNA de Transferência de Lisina/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/ultraestrutura
[Mh] Termos MeSH secundário: Transporte Biológico
Proteínas de Transporte de Cátions/metabolismo
Mitocôndrias/enzimologia
Complexos Multiproteicos/química
Complexos Multiproteicos/fisiologia
Fosfopiruvato Hidratase/metabolismo
RNA de Transferência/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (Multiprotein Complexes); 0 (RNA, Transfer, Lys); 0 (Saccharomyces cerevisiae Proteins); 136956-54-2 (TRK1 protein, S cerevisiae); 9014-25-9 (RNA, Transfer); EC 4.2.1.11 (Phosphopyruvate Hydratase); EC 6.1.1.6 (Lysine-tRNA Ligase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917110104


  2 / 623 MEDLINE  
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[PMID]:28783151
[Au] Autor:Nagao A; Ohara M; Miyauchi K; Yokobori SI; Yamagishi A; Watanabe K; Suzuki T
[Ad] Endereço:Department of Chemistry and Biotechnology, Graduate School of Engineering, University of Tokyo, Tokyo, Japan.
[Ti] Título:Hydroxylation of a conserved tRNA modification establishes non-universal genetic code in echinoderm mitochondria.
[So] Source:Nat Struct Mol Biol;24(9):778-782, 2017 Sep.
[Is] ISSN:1545-9985
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The genetic code is not frozen but still evolving, which can result in the acquisition of 'dialectal' codons that deviate from the universal genetic code. RNA modifications in the anticodon region of tRNAs play a critical role in establishing such non-universal genetic codes. In echinoderm mitochondria, the AAA codon specifies asparagine instead of lysine. By analyzing mitochondrial (mt-) tRNA isolated from the sea urchin (Mesocentrotus nudus), we discovered a novel modified nucleoside, hydroxy-N -threonylcarbamoyladenosine (ht A), 3' adjacent to the anticodon (position 37). Biochemical analysis revealed that ht A37 has the ability to prevent mt-tRNA from misreading AAA as lysine, thereby indicating that hydroxylation of N -threonylcarbamoyladenosine (t A) contributes to the establishment of the non-universal genetic code in echinoderm mitochondria.
[Mh] Termos MeSH primário: Echinacea/genética
Echinacea/metabolismo
Código Genético
Mitocôndrias/metabolismo
Processamento Pós-Transcricional do RNA
RNA de Transferência de Lisina/metabolismo
[Mh] Termos MeSH secundário: Asparagina/metabolismo
Hidroxilação
Lisina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Transfer, Lys); 7006-34-0 (Asparagine); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3449


  3 / 623 MEDLINE  
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[PMID]:28729369
[Au] Autor:Gill JS; Hardy SA; Blakely EL; Hopton S; Nemeth AH; Fratter C; Poulton J; Taylor RW; Downes SM
[Ad] Endereço:John Radcliffe Hospital, Oxford, UK.
[Ti] Título:Pigmentary retinopathy, rod-cone dysfunction and sensorineural deafness associated with a rare mitochondrial tRNA (m.8340G>A) gene variant.
[So] Source:Br J Ophthalmol;101(9):1298-1302, 2017 Sep.
[Is] ISSN:1468-2079
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: The rare mitochondrial DNA (mtDNA) variant m.8340G>A has been previously reported in the literature in a single, sporadic case of mitochondrial myopathy. In this report, we aim to investigate the case of a 39-year-old male patient with sensorineural deafness who presented to the eye clinic with nyctalopia, retinal pigmentary changes and bilateral cortical cataracts. METHODS: The patient was examined clinically and investigated with autofluorescence, full-field electroretinography, electro-oculogram and dark adaptometry. Sequencing of the mitochondrial genome in blood and muscle tissue was followed by histochemical and biochemical analyses together with single fibre studies of a muscle biopsy to confirm a mitochondrial aetiology. RESULTS: Electrophysiology, colour testing and dark adaptometry showed significant photoreceptor dysfunction with macular involvement. Sequencing the complete mitochondrial genome revealed a rare mitochondrial tRNA ( ) gene variant-m.8340G>A-which was heteroplasmic in blood (11%) and skeletal muscle (65%) and cosegregated with cytochrome oxidase-deficient fibres in single-fibre studies. CONCLUSION: We confirm the pathogenicity of the rare mitochondrial m.8340G>A variant the basis of single-fibre segregation studies and its association with an expanded clinical phenotype. Our case expands the phenotypic spectrum of diseases associated with mitochondrial tRNA point mutations, highlighting the importance of considering a mitochondrial diagnosis in similar cases presenting to the eye clinic and the importance of further genetic testing if standard mutational analysis does not yield a result.
[Mh] Termos MeSH primário: DNA Mitocondrial/genética
Células Fotorreceptoras de Vertebrados/patologia
Mutação Puntual
RNA de Transferência de Lisina/genética
Timidina Quinase/genética
Síndromes de Usher/genética
[Mh] Termos MeSH secundário: Adulto
Análise Mutacional de DNA
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Eletroculografia
Eletrorretinografia
Seres Humanos
Masculino
Mitocôndrias Musculares/enzimologia
Mitocôndrias Musculares/genética
Mitocôndrias Musculares/patologia
Músculo Esquelético/enzimologia
Músculo Esquelético/patologia
Imagem Óptica
Succinato Desidrogenase/metabolismo
Síndromes de Usher/diagnóstico
Síndromes de Usher/enzimologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (RNA, Transfer, Lys); EC 1.3.99.1 (Succinate Dehydrogenase); EC 1.9.3.1 (Electron Transport Complex IV); EC 2.7.1.- (thymidine kinase 2); EC 2.7.1.21 (Thymidine Kinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE
[do] DOI:10.1136/bjophthalmol-2017-310370


  4 / 623 MEDLINE  
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[PMID]:28351618
[Au] Autor:Chen R; Tu J; Liu Z; Meng F; Ma P; Ding Z; Yang C; Chen L; Deng X; Xie W
[Ad] Endereço:State Key Laboratory for Biocontrol, School of Life Sciences, The Sun Yat-Sen University, 135 W. Xingang Rd., Guangzhou, Guangdong 510275, People's Republic of China.
[Ti] Título:Structure of the MazF-mt9 toxin, a tRNA-specific endonuclease from Mycobacterium tuberculosis.
[So] Source:Biochem Biophys Res Commun;486(3):804-810, 2017 May 06.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tuberculosis (TB) is a severe disease caused by Mycobacterium tuberculosis (M. tb) and the well-characterized M. tb MazE/F proteins play important roles in stress adaptation. Recently, the MazF-mt9 toxin has been found to display endonuclease activities towards tRNAs but the mechanism is unknown. We hereby present the crystal structure of apo-MazF-mt9. The enzyme recognizes tRNA with a central UUU motif within the anticodon loop, but is insensitive to the sequence context outside of the loop. Based on our crystallographic and biochemical studies, we identified key residues for catalysis and proposed the potential tRNA-binding site.
[Mh] Termos MeSH primário: Anticódon/química
Apoproteínas/química
Proteínas de Bactérias/química
Toxinas Bacterianas/química
Endorribonucleases/química
Mycobacterium tuberculosis/química
RNA de Transferência de Lisina/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Apoproteínas/genética
Apoproteínas/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Toxinas Bacterianas/genética
Toxinas Bacterianas/metabolismo
Sequência de Bases
Sítios de Ligação
Clonagem Molecular
Endorribonucleases/genética
Endorribonucleases/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Modelos Moleculares
Mycobacterium tuberculosis/enzimologia
Mycobacterium tuberculosis/patogenicidade
Conformação de Ácido Nucleico
Ligação Proteica
Domínios Proteicos
Estrutura Secundária de Proteína
RNA de Transferência de Lisina/genética
RNA de Transferência de Lisina/metabolismo
Proteínas Recombinantes
Alinhamento de Sequência
Homologia Estrutural de Proteína
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticodon); 0 (Apoproteins); 0 (Bacterial Proteins); 0 (Bacterial Toxins); 0 (RNA, Transfer, Lys); 0 (Recombinant Proteins); EC 3.1.- (Endoribonucleases); EC 3.1.- (MazF protein, Mycobacterium tuberculosis)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170330
[St] Status:MEDLINE


  5 / 623 MEDLINE  
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[PMID]:28005340
[Au] Autor:Daskalova SM; Bhattacharya C; Dedkova LM; Hecht SM
[Ad] Endereço:Biodesign Center for BioEnergetics and School of Molecular Sciences, Arizona State University , Tempe, Arizona 85287, United States.
[Ti] Título:Probing the Flexibility of the Catalytic Nucleophile in the Lyase Catalytic Pocket of Human DNA Polymerase ß with Unnatural Lysine Analogues.
[So] Source:Biochemistry;56(3):500-513, 2017 Jan 24.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:DNA polymerase ß (Pol ß) is a key enzyme in mammalian base excision repair (BER), contributing stepwise 5'-deoxyribose phosphate (dRP) lyase and "gap-filling" DNA polymerase activities. The lyase reaction is believed to occur via a ß-elimination reaction following the formation of a Schiff base between the dRP group at the pre-incised apurinic/apyrimidinic site and the ε-amino group of Lys72. To probe the steric constraints on the formation and subsequent resolution of the putative Schiff base intermediate within the lyase catalytic pocket, Lys72 was replaced with each of several nonproteinogenic lysine analogues. The modified Pol ß enzymes were produced by coupled in vitro transcription and translation from a modified DNA template containing a TAG codon at the position corresponding to Lys72. In the presence of a misacylated tRNA transcript, suppression of the UAG codon in the transcribed mRNA led to elaboration of full length Pol ß having a lysine analogue at position 72. Replacement of the primary nucleophilic amine with a secondary amine in the form of N-methyllysine (4) affected mainly the stability of the Schiff base intermediate and resulted in relatively moderate inhibition of lyase activity and BER. Elongation of the side chain of the catalytic residue by one methylene group, achieved by introduction of homolysine (6) at position 72, apparently shifted the amino group to a position less favorable for Schiff base formation. Interestingly, this effect was attenuated when the side chain was elongated by replacing one side-chain methylene group with a bridging S atom (thialysine, 2). In comparison, replacement of lysine 72 with an analogue having a guanidine moiety in lieu of an ε-amino group (homoarginine, 5) or a sterically constrained secondary amine (piperidinylalanine, 3) led to almost complete suppression of dRP excision activity and the ability of Pol ß to support BER. These results help to define the tolerance of Pol ß to subtle local structural and functional alterations.
[Mh] Termos MeSH primário: DNA Polimerase beta/química
Reparo do DNA
Lisina/análogos & derivados
Fósforo-Oxigênio Liases/química
RNA de Transferência de Lisina/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Domínio Catalítico
Clonagem Molecular
Códon/genética
Códon/metabolismo
DNA/química
DNA/genética
DNA/metabolismo
DNA Polimerase beta/genética
DNA Polimerase beta/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Seres Humanos
Lisina/metabolismo
Modelos Moleculares
Fósforo-Oxigênio Liases/genética
Fósforo-Oxigênio Liases/metabolismo
Biossíntese de Proteínas
Domínios Proteicos
Estrutura Secundária de Proteína
RNA de Transferência de Lisina/genética
RNA de Transferência de Lisina/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Bases de Schiff/química
Bases de Schiff/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon); 0 (RNA, Transfer, Lys); 0 (Recombinant Proteins); 0 (Schiff Bases); 9007-49-2 (DNA); EC 2.7.7.- (5'-deoxyribose phosphate lyase); EC 2.7.7.- (DNA Polymerase beta); EC 4.6.- (Phosphorus-Oxygen Lyases); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00807


  6 / 623 MEDLINE  
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[PMID]:27799473
[Au] Autor:Kim HK; Tinoco I
[Ad] Endereço:Department of Chemistry, University of California, Berkeley, CA 94720, USA.
[Ti] Título:EF-G catalyzed translocation dynamics in the presence of ribosomal frameshifting stimulatory signals.
[So] Source:Nucleic Acids Res;45(5):2865-2874, 2017 Mar 17.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Programmed -1 ribosomal frameshifting (-1PRF) is tightly regulated by messenger RNA (mRNA) sequences and structures in expressing two or more proteins with precise ratios from a single mRNA. Using single-molecule fluorescence resonance energy transfer (smFRET) between (Cy5)EF-G and (Cy3)tRNALys, we studied the translational elongation dynamics of -1PRF in the Escherichia coli dnaX gene, which contains three frameshifting signals: a slippery sequence (A AAA AAG), a Shine-Dalgarno (SD) sequence and a downstream hairpin. The frameshift promoting signals mostly impair the EF-G-catalyzed translocation step of the two tRNALys and the slippery codons from the A- and P- sites. The hairpin acts as a road block slowing the translocation rate. The upstream SD sequence together with the hairpin promotes dissociation of futile EF-G and thus causes multiple EF-G driven translocation attempts. A slippery sequence also helps dissociation of the EF-G by providing alternative base-pairing options. These results indicate that frameshifting takes place during the repetitive ribosomal conformational changes associated with EF-G dissociation upon unsuccessful translocation attempts of the second slippage codon from the A- to the P- sites.
[Mh] Termos MeSH primário: Mudança da Fase de Leitura do Gene Ribossômico
Fator G para Elongação de Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Biocatálise
Códon
DNA Polimerase III/genética
Transferência Ressonante de Energia de Fluorescência
Mutação
Elongação Traducional da Cadeia Peptídica
RNA Mensageiro/química
RNA de Transferência de Lisina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Codon); 0 (DnaX protein, Bacteria); 0 (Peptide Elongation Factor G); 0 (RNA, Messenger); 0 (RNA, Transfer, Lys); EC 2.7.7.- (DNA Polymerase III)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161102
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1020


  7 / 623 MEDLINE  
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[PMID]:27908233
[Au] Autor:Smirnova EV; Chicherin IV; Baleva MV; Entelis NS; Tarassov IA; Kamenski PA
[Ad] Endereço:Lomonosov Moscow State University, Faculty of Biology, Moscow, 119991, Russia. kamenski_pa@mail.bio.msu.ru.
[Ti] Título:Procedure for Purification of Recombinant preMsk1p from E. coli Determines Its Properties as a Factor of tRNA Import into Yeast Mitochondria.
[So] Source:Biochemistry (Mosc);81(10):1081-1088, 2016 Oct.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial genomes of many eukaryotic organisms do not code for the full tRNA set necessary for organellar translation. Missing tRNA species are imported from the cytosol. In particular, one out of two cytosolic lysine tRNAs of the yeast Saccharomyces cerevisiae is partially internalized by mitochondria. The key protein factor of this process is the precursor of mitochondrial lysyl-tRNA synthetase, preMsk1p. In this work, we show that recombinant preMsk1p purified from E. coli in native conditions, when used in an in vitro tRNA import system, demonstrates some properties different from those shown by the renatured protein purified from E. coli in the denatured state. We also discuss the possible mechanistic reasons for this phenomenon.
[Mh] Termos MeSH primário: Lisina-tRNA Ligase
Mitocôndrias
Proteínas Mitocondriais
RNA Fúngico
RNA de Transferência de Lisina
Proteínas de Saccharomyces cerevisiae
Saccharomyces cerevisiae
[Mh] Termos MeSH secundário: Transporte Biológico Ativo
Escherichia coli/genética
Escherichia coli/metabolismo
Lisina-tRNA Ligase/química
Lisina-tRNA Ligase/genética
Lisina-tRNA Ligase/isolamento & purificação
Lisina-tRNA Ligase/metabolismo
Mitocôndrias/química
Mitocôndrias/genética
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/isolamento & purificação
Proteínas Mitocondriais/metabolismo
RNA Fúngico/química
RNA Fúngico/genética
RNA Fúngico/metabolismo
RNA de Transferência de Lisina/química
RNA de Transferência de Lisina/genética
RNA de Transferência de Lisina/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Saccharomyces cerevisiae/química
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/isolamento & purificação
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (RNA, Fungal); 0 (RNA, Transfer, Lys); 0 (Recombinant Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 6.1.1.6 (Lysine-tRNA Ligase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170113
[Lr] Data última revisão:
170113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161203
[St] Status:MEDLINE


  8 / 623 MEDLINE  
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[PMID]:27680513
[Au] Autor:Xiao X; Zhao B; Agris PF; Hall CK
[Ad] Endereço:Chemical and Biomolecular Engineering Department, North Carolina State University, Raleigh, North Carolina, 95-2767905.
[Ti] Título:Simulation study of the ability of a computationally-designed peptide to recognize target tRNA and other decoy tRNAs.
[So] Source:Protein Sci;25(12):2243-2255, 2016 Dec.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this paper, we investigate the ability of our computationally-designed peptide, Pept10 (PNWNGNRWLNNCLRG), to recognize the anticodon stem and loop (ASL) domain of the hypermodified tRNA (mcm s U ,ms t A ), a reverse transcription primer of HIV replication. Five other ASLs, the singly modified ASL (ms t A ), ASL (s U ), ASL (Ψ ), ASL (t A ), and ASL (s U ), were used as decoys. Explicit-solvent atomistic molecular dynamics simulations were performed to examine the process of binding of Pept10 with the target ASL (mcm s U ,ms t A ) and the decoy ASLs. Simulation results demonstrated that Pept10 is capable of recognizing the target ASL (mcm s U ,ms t A ) as well as one of the decoys, ASL (Ψ ), but screens out the other four decoy ASLs. The interchain van der Waals (VDW) and charge-charge (ELE + EGB) energies for the two best complexes were evaluated to shed light on the molecular recognition mechanism between Pept10 and ASLs. The results indicated that Pept10 recognizes and binds to the target ASL (mcm s U ,ms t A ) through residues W and R which interact with the nucleotides mcm s U , U , and ms t A via the interchain VDW energy. Pept10 also recognizes the decoy ASL (Ψ ) through residue R which contacts the nucleotide U via the interchain VDW energy. Regardless of the type of ASL, the positively charged arginines on Pept10 are attracted to the negatively charged phosphate linkages on the ASL via the interchain ELE + EGB energy, thereby enhancing the binding affinity.
[Mh] Termos MeSH primário: Simulação de Dinâmica Molecular
Peptídeos/química
RNA de Transferência de Lisina/química
Termodinâmica
[Mh] Termos MeSH secundário: Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (RNA, Transfer, Lys)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160930
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3056


  9 / 623 MEDLINE  
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[PMID]:27496282
[Au] Autor:Klassen R; Ciftci A; Funk J; Bruch A; Butter F; Schaffrath R
[Ad] Endereço:Institut für Biologie, Fachgebiet Mikrobiologie, Universität Kassel, Heinrich-Plett-Str. 40, D-34132 Kassel, Germany roland.klassen@uni-kassel.de.
[Ti] Título:tRNA anticodon loop modifications ensure protein homeostasis and cell morphogenesis in yeast.
[So] Source:Nucleic Acids Res;44(22):10946-10959, 2016 Dec 15.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Using budding yeast, we investigated a negative interaction network among genes for tRNA modifications previously implicated in anticodon-codon interaction: 5-methoxy-carbonyl-methyl-2-thio-uridine (mcm s U34: ELP3, URM1), pseudouridine (Ψ38/39: DEG1) and cyclic N6-threonyl-carbamoyl-adenosine (ct A37: TCD1). In line with functional cross talk between these modifications, we find that combined removal of either ct A37 or Ψ38/39 and mcm U34 or s U34 results in morphologically altered cells with synthetic growth defects. Phenotypic suppression by tRNA overexpression suggests that these defects are caused by malfunction of tRNA or tRNA , respectively. Indeed, mRNA translation and synthesis of the Gln-rich prion Rnq1 are severely impaired in the absence of Ψ38/39 and mcm U34 or s U34, and this defect can be rescued by overexpression of tRNA Surprisingly, we find that combined modification defects in the anticodon loops of different tRNAs induce similar cell polarity- and nuclear segregation defects that are accompanied by increased aggregation of cellular proteins. Since conditional expression of an artificial aggregation-prone protein triggered similar cytological aberrancies, protein aggregation is likely responsible for loss of morphogenesis and cytokinesis control in mutants with inappropriate tRNA anticodon loop modifications.
[Mh] Termos MeSH primário: RNA de Transferência de Glutamina/genética
RNA de Transferência de Lisina/genética
Saccharomycetales/genética
[Mh] Termos MeSH secundário: Anticódon/genética
Pareamento de Bases
Sequência de Bases
Genes Fúngicos
Homeostase
Morfogênese
Biossíntese de Proteínas
RNA Fúngico/genética
Saccharomycetales/citologia
Saccharomycetales/crescimento & desenvolvimento
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticodon); 0 (RNA, Fungal); 0 (RNA, Transfer, Gln); 0 (RNA, Transfer, Lys)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160807
[St] Status:MEDLINE


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[PMID]:27230773
[Au] Autor:Alves RM; da Silva Costa SM; do Amôr Divino Miranda PM; Ramos PZ; Marconi TG; Santos Oliveira G; Castilho AM; Sartorato EL
[Ad] Endereço:Center for Molecular and Genetic Engineering (CBMEG), University of Campinas (UNICAMP), Cidade Universitária Zeferino Vaz, Avenida Cândido Rondon 400, PO Box 6010, 13083-875, Campinas, São Paulo, Brazil.
[Ti] Título:Analysis of mitochondrial alterations in Brazilian patients with sensorineural hearing loss using MALDI-TOF mass spectrometry.
[So] Source:BMC Med Genet;17(1):41, 2016 May 26.
[Is] ISSN:1471-2350
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Mutations in the mitochondrial DNA (mtDNA) have been associated with aminoglycoside-induced and nonsyndromic deafness in different populations. In the present study, we investigated the contribution of mutations in mitochondrial genes to the etiology of hearing loss in a Brazilian sample. METHODS: Using mass spectrometry genotyping technology, combined with direct sequencing, 50 alterations previously described in 14 mitochondrial genes were screened in 152 patients with sensorineural hearing loss and in104 normal hearing controls. RESULTS: Fifteen known mitochondrial alterations were detected (G709A, A735G, A827G, G988A, A1555G, T4363C, T5628C, T5655C, G5821A, C7462T, G8363A, T10454C, G12236A, T1291C, G15927A). Pathogenic mutations in MT-RNR1 and MT-TK genes were detected in 3 % (5/152) of the patients with hearing loss. CONCLUSIONS: This study contributed to show the spectrum of mitochondrial variants in Brazilian patients with hearing loss. Frequency of A1555G was relatively high (2.6 %), indicating that this mutation is an important cause of hearing loss in our population. This work reports for the first time the investigation and the detection of the tRNA(Lys) G8363A mutation in Brazilian patients with maternally inherited sensorineural hearing loss.
[Mh] Termos MeSH primário: DNA Mitocondrial/análise
Perda Auditiva Neurossensorial/genética
Mitocôndrias/genética
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Mh] Termos MeSH secundário: Brasil
Estudos de Casos e Controles
DNA Mitocondrial/genética
DNA Mitocondrial/metabolismo
Feminino
Genótipo
Perda Auditiva Neurossensorial/patologia
Seres Humanos
Masculino
Membro 2 do Grupo A da Subfamília 4 de Receptores Nucleares/genética
RNA de Transferência de Lisina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Nuclear Receptor Subfamily 4, Group A, Member 2); 0 (RNA, Transfer, Lys)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160528
[St] Status:MEDLINE
[do] DOI:10.1186/s12881-016-0303-5



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