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[PMID]:28531275
[Au] Autor:Chetnani B; Mondragón A
[Ad] Endereço:Department of Molecular Biosciences, Northwestern University, 2205 Tech Drive, Evanston, IL 60208, USA.
[Ti] Título:Molecular envelope and atomic model of an anti-terminated glyQS T-box regulator in complex with tRNAGly.
[So] Source:Nucleic Acids Res;45(13):8079-8090, 2017 Jul 27.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A T-box regulator or riboswitch actively monitors the levels of charged/uncharged tRNA and participates in amino acid homeostasis by regulating genes involved in their utilization or biosynthesis. It has an aptamer domain for cognate tRNA recognition and an expression platform to sense the charge state and modulate gene expression. These two conserved domains are connected by a variable linker that harbors additional secondary structural elements, such as Stem III. The structural basis for specific tRNA binding is known, but the structural basis for charge sensing and the role of other elements remains elusive. To gain new structural insights on the T-box mechanism, a molecular envelope was calculated from small angle X-ray scattering data for the Bacillus subtilis glyQS T-box riboswitch in complex with an uncharged tRNAGly. A structural model of an anti-terminated glyQS T-box in complex with its cognate tRNAGly was derived based on the molecular envelope. It shows the location and relative orientation of various secondary structural elements. The model was validated by comparing the envelopes of the wild-type complex and two variants. The structural model suggests that in addition to a possible regulatory role, Stem III could aid in preferential stabilization of the T-box anti-terminated state allowing read-through of regulated genes.
[Mh] Termos MeSH primário: RNA Bacteriano/química
RNA Bacteriano/metabolismo
RNA de Transferência de Glicina/química
RNA de Transferência de Glicina/metabolismo
Riboswitch/genética
[Mh] Termos MeSH secundário: Bacillus subtilis/genética
Bacillus subtilis/metabolismo
Sequência de Bases
Modelos Moleculares
Conformação de Ácido Nucleico
RNA Bacteriano/genética
RNA de Transferência de Glicina/genética
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Bacterial); 0 (RNA, Transfer, Gly); 0 (Riboswitch)
[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:170523
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx451


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[PMID]:27261259
[Au] Autor:Qin X; Deng X; Chen L; Xie W
[Ad] Endereço:Key Laboratory of Gene Engineering of the Ministry of Education, 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; Center for Cellular and Structural Biology, The Sun Yat-Sen Universi
[Ti] Título:Crystal Structure of the Wild-Type Human GlyRS Bound with tRNA(Gly) in a Productive Conformation.
[So] Source:J Mol Biol;428(18):3603-14, 2016 Sep 11.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aminoacyl-tRNA synthetases are essential components of the protein translational machinery in all living species, among which the human glycyl-tRNA synthetase (hGlyRS) is of great research interest because of its unique species-specific aminoacylation properties and noncanonical roles in the Charcot-Marie-Tooth neurological disease. However, the molecular mechanisms of how the enzyme carries out its classical and alternative functions are not well understood. Here, we report a complex structure of the wild-type hGlyRS bound with tRNA(Gly) at 2.95Å. In the complex, the flexible Whep-TRS domain is visible in one of the subunits of the enzyme dimer, and the tRNA molecule is also completely resolved. At the active site, a glycyl-AMP molecule is synthesized and is waiting for the transfer of the glycyl moiety to occur. This cocrystal structure provides us with new details about the recognition mechanism in the intermediate stage during glycylation, which was not well elucidated in the previous crystal structures where the inhibitor AMPPNP was used for crystallization. More importantly, the structural and biochemical work conducted in the current and previous studies allows us to build a model of the full-length hGlyRS in complex with tRNA(Gly), which greatly helps us to understand the roles that insertions and the Whep-TRS domain play in the tRNA-binding process. Finally, through structure comparison with other class II aminoacyl-tRNA synthetases bound with their tRNA substrates, we found some commonalities of the aminoacylation mechanism between these enzymes.
[Mh] Termos MeSH primário: Glicina-tRNA Ligase/química
Glicina-tRNA Ligase/metabolismo
RNA de Transferência de Glicina/química
RNA de Transferência de Glicina/metabolismo
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Seres Humanos
Modelos Biológicos
Modelos Moleculares
Conformação de Ácido Nucleico
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Transfer, Gly); EC 6.1.1.14 (Glycine-tRNA Ligase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160605
[St] Status:MEDLINE


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[PMID]:27224426
[Au] Autor:Routh SB; Pawar KI; Ahmad S; Singh S; Suma K; Kumar M; Kuncha SK; Yadav K; Kruparani SP; Sankaranarayanan R
[Ad] Endereço:CSIR-Centre for Cellular and Molecular Biology, Hyderabad, India.
[Ti] Título:Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA Deacylase.
[So] Source:PLoS Biol;14(5):e1002465, 2016 May.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:D-aminoacyl-tRNA deacylase (DTD) removes D-amino acids mischarged on tRNAs and is thus implicated in enforcing homochirality in proteins. Previously, we proposed that selective capture of D-aminoacyl-tRNA by DTD's invariant, cross-subunit Gly-cisPro motif forms the mechanistic basis for its enantioselectivity. We now show, using nuclear magnetic resonance (NMR) spectroscopy-based binding studies followed by biochemical assays with both bacterial and eukaryotic systems, that DTD effectively misedits Gly-tRNAGly. High-resolution crystal structure reveals that the architecture of DTD's chiral proofreading site is completely porous to achiral glycine. Hence, L-chiral rejection is the only design principle on which DTD functions, unlike other chiral-specific enzymes such as D-amino acid oxidases, which are specific for D-enantiomers. Competition assays with elongation factor thermo unstable (EF-Tu) and DTD demonstrate that EF-Tu precludes Gly-tRNAGly misediting at normal cellular concentrations. However, even slightly higher DTD levels overcome this protection conferred by EF-Tu, thus resulting in significant depletion of Gly-tRNAGly. Our in vitro observations are substantiated by cell-based studies in Escherichia coli that show that overexpression of DTD causes cellular toxicity, which is largely rescued upon glycine supplementation. Furthermore, we provide direct evidence that DTD is an RNA-based catalyst, since it uses only the terminal 2'-OH of tRNA for catalysis without the involvement of protein side chains. The study therefore provides a unique paradigm of enzyme action for substrate selection/specificity by DTD, and thus explains the underlying cause of DTD's activity on Gly-tRNAGly. It also gives a molecular and functional basis for the necessity and the observed tight regulation of DTD levels, thereby preventing cellular toxicity due to misediting.
[Mh] Termos MeSH primário: Aminoaciltransferases/química
Aminoaciltransferases/metabolismo
Fator Tu de Elongação de Peptídeos/metabolismo
[Mh] Termos MeSH secundário: Alanina/química
Alanina/metabolismo
Aminoaciltransferases/genética
Domínio Catalítico
Cristalografia por Raios X
Proteínas de Drosophila/química
Proteínas de Drosophila/metabolismo
Escherichia coli/citologia
Escherichia coli/metabolismo
Proteínas de Escherichia coli/metabolismo
Glicina/química
Glicina/metabolismo
Hidrólise
Espectroscopia de Ressonância Magnética
Fator Tu de Elongação de Peptídeos/genética
Plasmodium falciparum/enzimologia
Aminoacil-RNA de Transferência/química
Aminoacil-RNA de Transferência/metabolismo
RNA de Transferência de Glicina/química
RNA de Transferência de Glicina/metabolismo
Ribossomos/metabolismo
Especificidade por Substrato
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Escherichia coli Proteins); 0 (RNA, Transfer, Amino Acyl); 0 (RNA, Transfer, Gly); 0 (Zebrafish Proteins); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (D-tyrosine tRNA(Tyr) deacylase); EC 3.6.1.- (Peptide Elongation Factor Tu); OF5P57N2ZX (Alanine); TE7660XO1C (Glycine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170621
[Lr] Data última revisão:
170621
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.1002465


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[PMID]:26865164
[Au] Autor:Li Q; Hu B; Hu GW; Chen CY; Niu X; Liu J; Zhou SM; Zhang CQ; Wang Y; Deng ZF
[Ad] Endereço:Institute of Microsurgery on Extremities, Shanghai Jiaotong University Affiliated Sixth People's Hospital, Shanghai 200233, China.
[Ti] Título:tRNA-Derived Small Non-Coding RNAs in Response to Ischemia Inhibit Angiogenesis.
[So] Source:Sci Rep;6:20850, 2016 Feb 11.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ischemic injuries will lead to necrotic tissue damage, and post-ischemia angiogenesis plays critical roles in blood flow restoration and tissue recovery. Recently, several types of small RNAs have been reported to be involved in this process. In this study, we first generated a rat brain ischemic model to investigate the involvement of new types of small RNAs in ischemia. We utilized deep sequencing and bioinformatics analyses to demonstrate that the level of small RNA fragments derived from tRNAs strikingly increased in the ischemic rat brain. Among these sequences, tRNA(Val)- and tRNA(Gly)-derived small RNAs account for the most abundant segments. The up-regulation of tRNA(Val)- and tRNA(Gly)-derived fragments was verified through northern blot and quantitative PCR analyses. The levels of these two fragments also increased in a mouse hindlimb ischemia model and cellular hypoxia model. Importantly, up-regulation of the tRNA(Val)- and tRNA(Gly)-derived fragments in endothelial cells inhibited cell proliferation, migration and tube formation. Furthermore, we showed that these small RNAs are generated by angiogenin cleavage. Our results indicate that tRNA-derived fragments are involved in tissue ischemia, and we demonstrate for the first time that tRNA(Val)- and tRNA(Gly)-derived fragments inhibit angiogenesis by modulating the function of endothelial cells.
[Mh] Termos MeSH primário: Isquemia Encefálica/genética
Neovascularização Fisiológica/genética
Pequeno RNA não Traduzido/genética
RNA de Transferência de Glicina/genética
RNA de Transferência de Valina/genética
[Mh] Termos MeSH secundário: Animais
Encéfalo/irrigação sanguínea
Encéfalo/metabolismo
Encéfalo/patologia
Isquemia Encefálica/metabolismo
Isquemia Encefálica/patologia
Hipóxia Celular
Movimento Celular
Proliferação Celular
Biologia Computacional
Regulação da Expressão Gênica
Membro Posterior/irrigação sanguínea
Membro Posterior/patologia
Células Endoteliais da Veia Umbilical Humana
Seres Humanos
Masculino
Camundongos
Proteólise
Clivagem do RNA
Pequeno RNA não Traduzido/metabolismo
RNA de Transferência de Glicina/metabolismo
RNA de Transferência de Valina/metabolismo
Ratos
Ratos Sprague-Dawley
Ribonuclease Pancreático/genética
Ribonuclease Pancreático/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Small Untranslated); 0 (RNA, Transfer, Gly); 0 (RNA, Transfer, Val); EC 3.1.27.- (angiogenin); EC 3.1.27.5 (Ribonuclease, Pancreatic)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160212
[St] Status:MEDLINE
[do] DOI:10.1038/srep20850


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[PMID]:26797133
[Au] Autor:Deng X; Qin X; Chen L; Jia Q; Zhang Y; Zhang Z; Lei D; Ren G; Zhou Z; Wang Z; Li Q; Xie W
[Ad] Endereço:From the State Key Laboratory for Biocontrol, School of Life Sciences, Sun Yat-Sen University, Guangzhou, Guangdong 510275, China, the Center for Cellular and Structural Biology and.
[Ti] Título:Large Conformational Changes of Insertion 3 in Human Glycyl-tRNA Synthetase (hGlyRS) during Catalysis.
[So] Source:J Biol Chem;291(11):5740-52, 2016 Mar 11.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glycyl-tRNA synthetase (GlyRS) is the enzyme that covalently links glycine to cognate tRNA for translation. It is of great research interest because of its nonconserved quaternary structures, unique species-specific aminoacylation properties, and noncanonical functions in neurological diseases, but none of these is fully understood. We report two crystal structures of human GlyRS variants, in the free form and in complex with tRNA(Gly) respectively, and reveal new aspects of the glycylation mechanism. We discover that insertion 3 differs considerably in conformation in catalysis and that it acts like a "switch" and fully opens to allow tRNA to bind in a cross-subunit fashion. The flexibility of the protein is supported by molecular dynamics simulation, as well as enzymatic activity assays. The biophysical and biochemical studies suggest that human GlyRS may utilize its flexibility for both the traditional function (regulate tRNA binding) and alternative functions (roles in diseases).
[Mh] Termos MeSH primário: Glicina-tRNA Ligase/química
Glicina-tRNA Ligase/metabolismo
RNA de Transferência de Glicina/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aminoacilação
Doença de Charcot-Marie-Tooth/enzimologia
Doença de Charcot-Marie-Tooth/genética
Cristalografia por Raios X
Glicina-tRNA Ligase/genética
Seres Humanos
Simulação de Dinâmica Molecular
Dados de Sequência Molecular
Mutação
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Transfer, Gly); EC 6.1.1.14 (Glycine-tRNA Ligase)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170311
[Lr] Data última revisão:
170311
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160123
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.679126


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[PMID]:26721685
[Au] Autor:Sharma U; Conine CC; Shea JM; Boskovic A; Derr AG; Bing XY; Belleannee C; Kucukural A; Serra RW; Sun F; Song L; Carone BR; Ricci EP; Li XZ; Fauquier L; Moore MJ; Sullivan R; Mello CC; Garber M; Rando OJ
[Ad] Endereço:Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA.
[Ti] Título:Biogenesis and function of tRNA fragments during sperm maturation and fertilization in mammals.
[So] Source:Science;351(6271):391-396, 2016 Jan 22.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Several recent studies link parental environments to phenotypes in subsequent generations. In this work, we investigate the mechanism by which paternal diet affects offspring metabolism. Protein restriction in mice affects small RNA (sRNA) levels in mature sperm, with decreased let-7 levels and increased amounts of 5' fragments of glycine transfer RNAs (tRNAs). In testicular sperm, tRNA fragments are scarce but increase in abundance as sperm mature in the epididymis. Epididymosomes (vesicles that fuse with sperm during epididymal transit) carry RNA payloads matching those of mature sperm and can deliver RNAs to immature sperm in vitro. Functionally, tRNA-glycine-GCC fragments repress genes associated with the endogenous retroelement MERVL, in both embryonic stem cells and embryos. Our results shed light on sRNA biogenesis and its dietary regulation during posttesticular sperm maturation, and they also link tRNA fragments to regulation of endogenous retroelements active in the preimplantation embryo.
[Mh] Termos MeSH primário: Fertilização
Regulação da Expressão Gênica
RNA de Transferência de Glicina/metabolismo
RNA de Transferência de Glicina/fisiologia
Maturação do Esperma
Espermatozoides/metabolismo
[Mh] Termos MeSH secundário: Animais
Blastocisto/metabolismo
Dieta com Restrição de Proteínas
Epididimo/metabolismo
Masculino
Camundongos
MicroRNAs/metabolismo
Retroelementos/genética
Testículo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (MicroRNAs); 0 (RNA, Transfer, Gly); 0 (Retroelements); 0 (mirnlet7 microRNA, mouse)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160102
[St] Status:MEDLINE
[do] DOI:10.1126/science.aad6780


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[PMID]:26276802
[Au] Autor:Apostolidi M; Saad NY; Drainas D; Pournaras S; Becker HD; Stathopoulos C
[Ad] Endereço:Department of Biochemistry, School of Medicine, University of Patras, 26504 Patras, Greece.
[Ti] Título:A glyS T-box riboswitch with species-specific structural features responding to both proteinogenic and nonproteinogenic tRNAGly isoacceptors.
[So] Source:RNA;21(10):1790-806, 2015 Oct.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Staphylococcus aureus, a T-box riboswitch exists upstream of the glyS gene to regulate transcription of the sole glycyl-tRNA synthetase, which aminoacylates five tRNA(Gly) isoacceptors bearing GCC or UCC anticodons. Subsequently, the glycylated tRNAs serve as substrates for decoding glycine codons during translation, and also as glycine donors for exoribosomal synthesis of pentaglycine peptides during cell wall formation. Probing of the predicted T-box structure revealed a long stem I, lacking features previously described for similar T-boxes. Moreover, the antiterminator stem includes a 42-nt long intervening sequence, which is staphylococci-specific. Finally, the terminator conformation adopts a rigid two-stem structure, where the intervening sequence forms the first stem followed by the second stem, which includes the more conserved residues. Interestingly, all five tRNA(Gly) isoacceptors interact with S. aureus glyS T-box with different binding affinities and they all induce transcription readthrough at different levels. The ability of both GCC and UCC anticodons to interact with the specifier loop indicates ambiguity during the specifier triplet reading, similar to the unconventional reading of glycine codons during protein synthesis. The S. aureus glyS T-box structure is consistent with the recent crystallographic and NMR studies, despite apparent differences, and highlights the phylogenetic variability of T-boxes when studied in a genome-dependent context. Our data suggest that the S. aureus glyS T-box exhibits differential tRNA selectivity, which possibly contributes toward the regulation and synchronization of ribosomal and exoribosomal peptide synthesis, two essential but metabolically unrelated pathways.
[Mh] Termos MeSH primário: Proteínas/metabolismo
RNA de Transferência de Glicina/metabolismo
Riboswitch
[Mh] Termos MeSH secundário: Sequência de Bases
Dados de Sequência Molecular
Conformação de Ácido Nucleico
RNA de Transferência de Glicina/química
Homologia de Sequência do Ácido Nucleico
Staphylococcus aureus/genética
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proteins); 0 (RNA, Transfer, Gly); 0 (Riboswitch)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150816
[St] Status:MEDLINE
[do] DOI:10.1261/rna.052712.115


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[PMID]:26229106
[Au] Autor:Caserta E; Liu LC; Grundy FJ; Henkin TM
[Ad] Endereço:From the Department of Microbiology and Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210.
[Ti] Título:Codon-Anticodon Recognition in the Bacillus subtilis glyQS T Box Riboswitch: RNA-DEPENDENT CODON SELECTION OUTSIDE THE RIBOSOME.
[So] Source:J Biol Chem;290(38):23336-47, 2015 Sep 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many amino acid-related genes in Gram-positive bacteria are regulated by the T box riboswitch. The leader RNA of genes in the T box family controls the expression of downstream genes by monitoring the aminoacylation status of the cognate tRNA. Previous studies identified a three-nucleotide codon, termed the "Specifier Sequence," in the riboswitch that corresponds to the amino acid identity of the downstream genes. Pairing of the Specifier Sequence with the anticodon of the cognate tRNA is the primary determinant of specific tRNA recognition. This interaction mimics codon-anticodon pairing in translation but occurs in the absence of the ribosome. The goal of the current study was to determine the effect of a full range of mismatches for comparison with codon recognition in translation. Mutations were individually introduced into the Specifier Sequence of the glyQS leader RNA and tRNA(Gly) anticodon to test the effect of all possible pairing combinations on tRNA binding affinity and antitermination efficiency. The functional role of the conserved purine 3' of the Specifier Sequence was also verifiedin this study. We found that substitutions at the Specifier Sequence resulted in reduced binding, the magnitude of which correlates well with the predicted stability of the RNA-RNA pairing. However, the tolerance for specific mismatches in antitermination was generally different from that during decoding, which reveals a unique tRNA recognition pattern in the T box antitermination system.
[Mh] Termos MeSH primário: Anticódon/química
Bacillus subtilis/química
Códon/química
RNA Bacteriano/química
RNA de Transferência de Glicina/química
Riboswitch/fisiologia
[Mh] Termos MeSH secundário: Anticódon/genética
Anticódon/metabolismo
Bacillus subtilis/genética
Bacillus subtilis/metabolismo
Proteínas de Bactérias/biossíntese
Códon/genética
Códon/metabolismo
Biossíntese de Proteínas/fisiologia
RNA Bacteriano/genética
RNA Bacteriano/metabolismo
RNA de Transferência de Glicina/genética
RNA de Transferência de Glicina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Anticodon); 0 (Bacterial Proteins); 0 (Codon); 0 (RNA, Bacterial); 0 (RNA, Transfer, Gly); 0 (Riboswitch)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:161025
[Lr] Data última revisão:
161025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150801
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.673236


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[PMID]:26134044
[Au] Autor:Li W; Wen C; Li W; Wang H; Guan X; Zhang W; Ye W; Lu J
[Ad] Endereço:Key Laboratory of Laboratory Medicine, Ministry of Education, Wenzhou, 325035, Zhejiang, People's Republic of China.
[Ti] Título:The tRNA(Gly) T10003C mutation in mitochondrial haplogroup M11b in a Chinese family with diabetes decreases the steady-state level of tRNA(Gly), increases aberrant reactive oxygen species production, and reduces mitochondrial membrane potential.
[So] Source:Mol Cell Biochem;408(1-2):171-9, 2015 Oct.
[Is] ISSN:1573-4919
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondrial diabetes originates mainly from mutations located in maternally transmitted, mitochondrial tRNA-coding genes. In a genetic screening program of type 2 diabetes conducted with a Chinese Han population, we found one family with suggestive maternally transmitted diabetes. The proband's mitochondrial genome was analyzed using DNA sequencing. Total 42 known nucleoside changes and 1 novel variant were identified, and the entire mitochondrial DNA sequence was assigned to haplogroup M11b. Phylogenetic analysis showed that a homoplasmic mutation, 10003T>C transition, occurred at the highly conserved site in the gene encoding tRNA(Gly). Using a transmitochondrial cybrid cell line harboring this mutation, we observed that the steady-state level of tRNA(Gly) significantly affected and the amount of tRNA(Gly) decreased by 97%, production of reactive oxygen species was enhanced, and mitochondrial membrane potential, mtDNA copy number and cellular oxygen consumption rate were remarkably decreased compared with wild-type cybrid cells. The homoplasmic 10003T>C mutation in the mitochondrial tRNA(Gly) gene suggested to be as a pathogenesis-related mutation which might contribute to the maternal inherited diabetes in the Han Chinese family.
[Mh] Termos MeSH primário: Grupo com Ancestrais do Continente Asiático/genética
Diabetes Mellitus Tipo 2/genética
Mitocôndrias/genética
Doenças Mitocondriais/genética
Mutação
RNA de Transferência de Glicina/genética
[Mh] Termos MeSH secundário: Idoso
Grupo com Ancestrais do Continente Asiático/etnologia
China/etnologia
Diabetes Mellitus Tipo 2/etnologia
Feminino
Predisposição Genética para Doença
Genoma Mitocondrial
Haplótipos
Seres Humanos
Masculino
Potencial da Membrana Mitocondrial
Meia-Idade
Consumo de Oxigênio
Linhagem
Filogenia
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA, Transfer, Gly); 0 (Reactive Oxygen Species)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150703
[St] Status:MEDLINE
[do] DOI:10.1007/s11010-015-2493-0


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[PMID]:25940616
[Au] Autor:Tosar JP; Gámbaro F; Sanguinetti J; Bonilla B; Witwer KW; Cayota A
[Ad] Endereço:Functional Genomics Unit, Institut Pasteur de Montevideo, Montevideo 11400, Uruguay Nuclear Research Center, Faculty of Science, Universidad de la República, Montevideo 11400, Uruguay.
[Ti] Título:Assessment of small RNA sorting into different extracellular fractions revealed by high-throughput sequencing of breast cell lines.
[So] Source:Nucleic Acids Res;43(11):5601-16, 2015 Jun 23.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Intercellular communication can be mediated by extracellular small regulatory RNAs (sRNAs). Circulating sRNAs are being intensively studied for their promising use as minimally invasive disease biomarkers. To date, most attention is centered on exosomes and microRNAs as the vectors and the secreted species, respectively. However, this field would benefit from an increased understanding of the plethora of sRNAs secreted by different cell types in different extracellular fractions. It is still not clear if specific sRNAs are selected for secretion, or if sRNA secretion is mostly passive. We sequenced the intracellular sRNA content (19-60 nt) of breast epithelial cell lines (MCF-7 and MCF-10A) and compared it with extracellular fractions enriched in microvesicles, exosomes and ribonucleoprotein complexes. Our results are consistent with a non-selective secretion model for most microRNAs, although a few showed secretion patterns consistent with preferential secretion. On the contrary, 5' tRNA halves and 5' RNA Y4-derived fragments of 31-33 were greatly and significantly enriched in the extracellular space (even in non-mammary cell lines), where tRNA halves were detected as part of ∼45 kDa ribonucleoprotein complexes. Overall, we show that different sRNA families have characteristic secretion patterns and open the question of the role of these sRNAs in the extracellular space.
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Espaço Extracelular/genética
Pequeno RNA não Traduzido/secreção
[Mh] Termos MeSH secundário: Neoplasias da Mama/secreção
Linhagem Celular Tumoral
Feminino
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
Células MCF-7
MicroRNAs/metabolismo
Pequeno RNA não Traduzido/análise
RNA de Transferência de Ácido Glutâmico/isolamento & purificação
RNA de Transferência de Glicina/isolamento & purificação
Ribonucleoproteínas/isolamento & purificação
Análise de Sequência de RNA
Vesículas Transportadoras/secreção
Vesículas Transportadoras/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (MicroRNAs); 0 (RNA, Small Untranslated); 0 (RNA, Transfer, Glu); 0 (RNA, Transfer, Gly); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150506
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkv432



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