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  1 / 3161 MEDLINE  
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[PMID]:29188663
[Au] Autor:Lü YH; Ma KJ; Li ZH; Gu J; Bao JY; Yang ZF; Gao J; Zeng Y; Tao L; Chen L
[Ad] Endereço:Shanghai University of Medicine & Health Science, Shanghai 201318, China.
[Ti] Título:[Correlation between RNA Expression Level and Early PMI in Human Brain Tissue].
[So] Source:Fa Yi Xue Za Zhi;32(4):245-249, 2016 Aug.
[Is] ISSN:1004-5619
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVES: To explore the correlation between the expression levels of several RNA markers in human brain tissue and early postmortem interval (PMI). METHODS: Twelve individuals with known PMI (range from 4.3 to 22.5 h) were selected and total RNA was extracted from brain tissue. Eight commonly used RNA markers were chosen including -actin, GAPDH, RPS29, 18S rRNA, 5S rRNA, U6 snRNA, miRNA-9 and miRNA-125b, and the expression levels were detected in brain tissue by real-time fluorescent quantitative PCR. The internal reference markers with stable expression in early PMI were screened using geNorm software and the relationship between its expression level and some relevant factors such as age, gender and cause of death were analyzed. RNA markers normalized by internal reference were inserted into the mathematic model established by previous research for PMI estimation using R software. Model quality was judged by the error rate calculated with estimated PMI. RESULTS: 5S rRNA, miRNA-9 and miRNA-125b showed quite stable expression and their expression levels had no relation with age, gender and cause of death. The error rate of estimated PMI using -actin was 24.6%, while GAPDH was 41.0%. CONCLUSIONS: 5S rRNA, miRNA-9 and miRNA-125b are suitable as internal reference markers of human brain tissue owing to their stable expression in early PMI. The expression level of -actin correlates well with PMI, which can be used as an additional index for early PMI estimation.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
MicroRNAs/análise
Mudanças Depois da Morte
RNA Nuclear Pequeno/análise
[Mh] Termos MeSH secundário: Actinas/análise
Autopsia
Seres Humanos
Modelos Teóricos
Estabilidade de RNA
RNA Ribossômico 18S/análise
RNA Ribossômico 5S/análise
Reação em Cadeia da Polimerase em Tempo Real
Software
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (MicroRNAs); 0 (RNA, Ribosomal, 18S); 0 (RNA, Ribosomal, 5S); 0 (RNA, Small Nuclear); 0 (U6 small nuclear RNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.3969/j.issn.1004-5619.2016.04.002


  2 / 3161 MEDLINE  
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[PMID]:28468917
[Au] Autor:Aitken S; Semple CA
[Ad] Endereço:MRC Human Genetics Unit, Institute of Genetics and Molecular Medicine, University of Edinburgh, Edinburgh EH4 2XU, UK stuart.aitken@igmm.ed.ac.uk.
[Ti] Título:The circadian dynamics of small nucleolar RNA in the mouse liver.
[So] Source:J R Soc Interface;14(130), 2017 May.
[Is] ISSN:1742-5662
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The circadian regulation of gene expression allows plants and animals to anticipate predictable environmental changes. While the influence of the circadian clock has recently been shown to extend to ribosome biogenesis, the dynamics and regulation of the many small nucleolar RNA that are required in pre-ribosomal RNA folding and modification are unknown. Using a novel computational method, we show that 18S and 28S pre-rRNA are subject to circadian regulation in a nuclear RNA sequencing time course. A population of snoRNA with circadian expression is identified that is functionally associated with rRNA modification. More generally, we find the abundance of snoRNA known to modify 18S and 28S to be inversely correlated with the abundance of their target. Cyclic patterns in the expression of a number of snoRNA indicate a coordination with rRNA maturation, potentially through an upregulation in their biogenesis, or their release from mature rRNA at the end of the previous cycle of rRNA maturation, in antiphase with the diurnal peak in pre-rRNA. Few cyclic snoRNA have cyclic host genes, indicating the action of regulatory mechanisms in addition to transcriptional activation of the host gene. For highly expressed independently transcribed snoRNA, we find a characteristic RNA polymerase II and H3K4me3 signature that correlates with mean snoRNA expression over the day.
[Mh] Termos MeSH primário: Ritmo Circadiano/fisiologia
Regulação da Expressão Gênica/fisiologia
Fígado/metabolismo
Modelos Biológicos
RNA Nuclear Pequeno/biossíntese
[Mh] Termos MeSH secundário: Animais
Camundongos
RNA Ribossômico 18S/biossíntese
RNA Ribossômico 28S/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Ribosomal, 18S); 0 (RNA, Ribosomal, 28S); 0 (RNA, Small Nuclear)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  3 / 3161 MEDLINE  
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[PMID]:29066300
[Au] Autor:Gong Q; Stump MR; Zhou Z
[Ad] Endereço:Knight Cardiovascular Institute, Oregon Health & Science University, Portland, OR, United States.
[Ti] Título:Upregulation of functional Kv11.1a isoform expression by modified U1 small nuclear RNA.
[So] Source:Gene;641:220-225, 2018 Jan 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The KCNH2 or human ether-a go-go-related gene (hERG) encodes the Kv11.1 potassium channel that conducts the rapidly activating delayed rectifier potassium current in the heart. The expression of Kv11.1 C-terminal isoforms is directed by the alternative splicing and polyadenylation of intron 9. Splicing of intron 9 leads to the formation of a functional, full-length Kv11.1a isoform and polyadenylation of intron 9 results in the production of a non-functional, C-terminally truncated Kv11.1a-USO isoform. The relative expression of Kv11.1a and Kv11.1a-USO plays an important role in regulating Kv11.1 channel function. In the heart, only one-third of KCNH2 pre-mRNA is processed to Kv11.1a due to the weak 5' splice site of intron 9. We previously showed that the weak 5' splice site is caused by sequence deviation from the consensus, and that mutations toward the consensus sequence increased the efficiency of intron 9 splicing. It is well established that 5' splice sites are recognized by complementary base-paring with U1 small nuclear RNA (U1 snRNA). In this study, we modified the sequence of U1 snRNA to increase its complementarity to the 5' splice site of KCNH2 intron 9 and observed a significant increase in the efficiency of intron 9 splicing. RNase protection assay and western blot analysis showed that modified U1 snRNA increased the expression of the functional Kv11.1a isoform and concomitantly decreased the expression of the non-functional Kv11.1a-USO isoform. In patch-clamp experiments, modified U1 snRNA significantly increased Kv11.1 current. Our findings suggest that relative expression of Kv11.1 C-terminal isoforms can be regulated by modified U1 snRNA.
[Mh] Termos MeSH primário: Canal de Potássio ERG1/genética
RNA Nuclear Pequeno/genética
Regulação para Cima/genética
[Mh] Termos MeSH secundário: Processamento Alternativo/genética
Linhagem Celular
Células HEK293
Seres Humanos
Íntrons/genética
Poliadenilação/genética
Isoformas de Proteínas/genética
Precursores de RNA/genética
Sítios de Splice de RNA/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ERG1 Potassium Channel); 0 (KCNH2 protein, human); 0 (Protein Isoforms); 0 (RNA Precursors); 0 (RNA Splice Sites); 0 (RNA, Small Nuclear); 0 (U1 small nuclear RNA)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171026
[St] Status:MEDLINE


  4 / 3161 MEDLINE  
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[PMID]:29368487
[Au] Autor:Trifonova AA; Filyushin MA; Kochieva EZ; Kudryavtsev AM
[Ti] Título:[Analysis of the ITS1/ITS2 nuclear spacers and the secondary structure of 5.8S rRNA gene in endemic species Bellevalia sarmatica (Pall. ex Georgi) Woronow and related species of the subfamily scilloideae].
[So] Source:Genetika;52(5):605-10, 2016 May.
[Is] ISSN:0016-6758
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:Sequence variability of the ITS spacers and 5.8S rRNA gene was examined in 11 accessions of the subfamily Scilloideae, including seven accessions of rare and endangered species Bellevalia sarmatica from Volgograd region. The intraspecific polymorphism level of the examined ITS1­5.8S­ITS2 sequence of B. sarmatica accessions constituted 1.3%. The phylogenetic position of B. sarmatica within the genus Bellevalia was determined. It was demonstrated that B. sarmatica belonged to the section Nutantes, and the most closely related species were B. webbiana and B. dubia. Nucleotide substitutions in the 5.8S rRNA gene sequence of the analyzed Scilloideae accessions were identified and studied. The predicted secondary structure of 5.8S rRNA gene was constructed. It was demonstrated that in the examined accessions, mutations in the 5.8S rRNA gene were mainly localized in the third hairpin region and had no effect on the secondary structure of the 5.8S rRNA molecule.
[Mh] Termos MeSH primário: Asparagales/genética
Variação Genética
Conformação de Ácido Nucleico
RNA Nuclear Pequeno/genética
[Mh] Termos MeSH secundário: Asparagales/química
RNA Nuclear Pequeno/química
Federação Russa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Small Nuclear); 0 (U4 small nuclear RNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


  5 / 3161 MEDLINE  
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[PMID]:28747322
[Au] Autor:Panchapakesan SSS; Ferguson ML; Hayden EJ; Chen X; Hoskins AA; Unrau PJ
[Ad] Endereço:Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
[Ti] Título:Ribonucleoprotein purification and characterization using RNA Mango.
[So] Source:RNA;23(10):1592-1599, 2017 10.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The characterization of RNA-protein complexes (RNPs) is a difficult but increasingly important problem in modern biology. By combining the compact RNA Mango aptamer with a fluorogenic thiazole orange desthiobiotin (TO1-Dtb or TO3-Dtb) ligand, we have created an RNA tagging system that simplifies the purification and subsequent characterization of endogenous RNPs. Mango-tagged RNP complexes can be immobilized on a streptavidin solid support and recovered in their native state by the addition of free biotin. Furthermore, Mango-based RNP purification can be adapted to different scales of RNP isolation ranging from pull-down assays to the isolation of large amounts of biochemically defined cellular RNPs. We have incorporated the Mango aptamer into the U1 small nuclear RNA (snRNA), shown that the Mango-snRNA is functional in cells, and used the aptamer to pull down a U1 snRNA-associated protein. To demonstrate large-scale isolation of RNPs, we purified and characterized bacterial RNA polymerase holoenzyme (HE) in complex with a Mango-containing 6S RNA. We were able to use the combination of a red-shifted TO3-Dtb ligand and eGFP-tagged HE to follow the binding and release of the 6S RNA by two-color native gel analysis as well as by single-molecule fluorescence cross-correlation spectroscopy. Together these experiments demonstrate how the Mango aptamer in conjunction with simple derivatives of its flurophore ligands enables the purification and characterization of endogenous cellular RNPs in vitro.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/química
Bioquímica/métodos
Ribonucleoproteínas/isolamento & purificação
Espectrometria de Fluorescência/métodos
[Mh] Termos MeSH secundário: Benzotiazóis/química
Biotina/análogos & derivados
Biotina/química
Proteínas de Fluorescência Verde/genética
Quinolinas/química
RNA Bacteriano/metabolismo
RNA Nuclear Pequeno/química
RNA não Traduzido/metabolismo
Ribonucleoproteínas/metabolismo
Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (6S RNA); 0 (Aptamers, Nucleotide); 0 (Benzothiazoles); 0 (Quinolines); 0 (RNA, Bacterial); 0 (RNA, Small Nuclear); 0 (RNA, Untranslated); 0 (Ribonucleoproteins); 0 (U1 small nuclear RNA); 107091-89-4 (thiazole orange); 147336-22-9 (Green Fluorescent Proteins); 6SO6U10H04 (Biotin); 71U5JB52KS (desthiobiotin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1261/rna.062166.117


  6 / 3161 MEDLINE  
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[PMID]:28934473
[Au] Autor:Yeh CS; Chang SL; Chen JH; Wang HK; Chou YC; Wang CH; Huang SH; Larson A; Pleiss JA; Chang WH; Chang TH
[Ad] Endereço:Institute of Biochemistry and Molecular Biology, National Yang-Ming University, Taipei, Taiwan.
[Ti] Título:The conserved AU dinucleotide at the 5' end of nascent U1 snRNA is optimized for the interaction with nuclear cap-binding-complex.
[So] Source:Nucleic Acids Res;45(16):9679-9693, 2017 Sep 19.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Splicing is initiated by a productive interaction between the pre-mRNA and the U1 snRNP, in which a short RNA duplex is established between the 5' splice site of a pre-mRNA and the 5' end of the U1 snRNA. A long-standing puzzle has been why the AU dincucleotide at the 5'-end of the U1 snRNA is highly conserved, despite the absence of an apparent role in the formation of the duplex. To explore this conundrum, we varied this AU dinucleotide into all possible permutations and analyzed the resulting molecular consequences. This led to the unexpected findings that the AU dinucleotide dictates the optimal binding of cap-binding complex (CBC) to the 5' end of the nascent U1 snRNA, which ultimately influences the utilization of U1 snRNP in splicing. Our data also provide a structural interpretation as to why the AU dinucleotide is conserved during evolution.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Cap de RNA/metabolismo
RNA Nuclear Pequeno/química
RNA Nuclear Pequeno/metabolismo
[Mh] Termos MeSH secundário: Pareamento de Bases
Simulação de Acoplamento Molecular
Complexo Proteico Nuclear de Ligação ao Cap/genética
Complexo Proteico Nuclear de Ligação ao Cap/metabolismo
Proteínas de Ligação ao Cap de RNA/genética
Precursores de RNA/metabolismo
Processamento de RNA
RNA Nuclear Pequeno/genética
Ribonucleoproteína Nuclear Pequena U1/genética
Ribonucleoproteína Nuclear Pequena U1/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Leveduras/genética
Leveduras/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CBC2 protein, S cerevisiae); 0 (Nuclear Cap-Binding Protein Complex); 0 (RNA Cap-Binding Proteins); 0 (RNA Precursors); 0 (RNA, Small Nuclear); 0 (Ribonucleoprotein, U1 Small Nuclear); 0 (Saccharomyces cerevisiae Proteins); 0 (U1 small nuclear RNA)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx608


  7 / 3161 MEDLINE  
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[PMID]:28919079
[Au] Autor:Wan R; Yan C; Bai R; Lei J; Shi Y
[Ad] Endereço:Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China.
[Ti] Título:Structure of an Intron Lariat Spliceosome from Saccharomyces cerevisiae.
[So] Source:Cell;171(1):120-132.e12, 2017 Sep 21.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The disassembly of the intron lariat spliceosome (ILS) marks the end of a splicing cycle. Here we report a cryoelectron microscopy structure of the ILS complex from Saccharomyces cerevisiae at an average resolution of 3.5 Å. The intron lariat remains bound in the spliceosome whereas the ligated exon is already dissociated. The step II splicing factors Prp17 and Prp18, along with Cwc21 and Cwc22 that stabilize the 5' exon binding to loop I of U5 small nuclear RNA (snRNA), have been released from the active site assembly. The DEAH family ATPase/helicase Prp43 binds Syf1 at the periphery of the spliceosome, with its RNA-binding site close to the 3' end of U6 snRNA. The C-terminal domain of Ntr1/Spp382 associates with the GTPase Snu114, and Ntr2 is anchored to Prp8 while interacting with the superhelical domain of Ntr1. These structural features suggest a plausible mechanism for the disassembly of the ILS complex.
[Mh] Termos MeSH primário: Íntrons
Spliceossomos/ultraestrutura
[Mh] Termos MeSH secundário: Microscopia Crioeletrônica
RNA Helicases DEAD-box/química
Modelos Moleculares
Precursores de RNA/química
Precursores de RNA/ultraestrutura
RNA Nuclear Pequeno/química
RNA Nuclear Pequeno/ultraestrutura
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/química
Schizosaccharomyces/química
Spliceossomos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA Precursors); 0 (RNA, Small Nuclear); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (PRP43 protein, S cerevisiae); EC 3.6.4.13 (DEAD-box RNA Helicases)
[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:170919
[St] Status:MEDLINE


  8 / 3161 MEDLINE  
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[PMID]:28838205
[Au] Autor:Henning LM; Santos KF; Sticht J; Jehle S; Lee CT; Wittwer M; Urlaub H; Stelzl U; Wahl MC; Freund C
[Ad] Endereço:Laboratory of Protein Biochemistry, Institute for Chemistry and Biochemistry, Freie Universität Berlin, Thielallee 63, Berlin 14195, Germany.
[Ti] Título:A new role for FBP21 as regulator of Brr2 helicase activity.
[So] Source:Nucleic Acids Res;45(13):7922-7937, 2017 Jul 27.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Splicing of eukaryotic pre-mRNA is carried out by the spliceosome, which assembles stepwise on each splicing substrate. This requires the concerted action of snRNPs and non-snRNP accessory proteins, the functions of which are often not well understood. Of special interest are B complex factors that enter the spliceosome prior to catalytic activation and may alter splicing kinetics and splice site selection. One of these proteins is FBP21, for which we identified several spliceosomal binding partners in a yeast-two-hybrid screen, among them the RNA helicase Brr2. Biochemical and biophysical analyses revealed that an intrinsically disordered region of FBP21 binds to an extended surface of the C-terminal Sec63 unit of Brr2. Additional contacts in the C-terminal helicase cassette are required for allosteric inhibition of Brr2 helicase activity. Furthermore, the direct interaction between FBP21 and the U4/U6 di-snRNA was found to reduce the pool of unwound U4/U6 di-snRNA. Our results suggest FBP21 as a novel key player in the regulation of Brr2.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Proteínas Nucleares/metabolismo
RNA Helicases/metabolismo
Ribonucleoproteínas Nucleares Pequenas/metabolismo
[Mh] Termos MeSH secundário: Regulação Alostérica
Sequência de Aminoácidos
Proteínas de Transporte/química
Proteínas de Transporte/genética
Seres Humanos
Modelos Moleculares
Proteínas Nucleares/química
Proteínas Nucleares/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
RNA Helicases/química
RNA Helicases/genética
Precursores de RNA/metabolismo
Processamento de RNA
RNA Nuclear Pequeno/metabolismo
Ribonucleoproteínas Nucleares Pequenas/química
Ribonucleoproteínas Nucleares Pequenas/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Spliceossomos/metabolismo
Técnicas do Sistema de Duplo-Híbrido
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Nuclear Proteins); 0 (Peptide Fragments); 0 (RNA Precursors); 0 (RNA, Small Nuclear); 0 (Ribonucleoproteins, Small Nuclear); 0 (SNRNP200 protein, human); 0 (Saccharomyces cerevisiae Proteins); 0 (U4 small nuclear RNA); 0 (U6 small nuclear RNA); 0 (WBP4 protein, human); EC 3.6.4.13 (RNA Helicases)
[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:170826
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx535


  9 / 3161 MEDLINE  
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[PMID]:28777948
[Au] Autor:Bensaude O
[Ad] Endereço:IBENS-CNRS UMR 8197-INSERM U1024-Ecole Normale Supérieure 46, Rue d'Ulm, Cedex 05, 75230 Paris, France. Electronic address: bensaude@biologie.ens.fr.
[Ti] Título:HEXIM1 Has Different Functions within Different RNA-Protein Complexes.
[So] Source:Mol Cell;67(3):357-359, 2017 Aug 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this issue of Molecular Cell, Morchikh et al. (2017) describe a new ribonuclear complex built around HEXIM1 and the long non-coding RNA NEAT1. This complex regulates the innate immune response to DNA viruses and is distinct from the HEXIM1-7SK RNA complex that regulates transcription elongation.
[Mh] Termos MeSH primário: Fator B de Elongação Transcricional Positiva/genética
Proteínas de Ligação a RNA/genética
[Mh] Termos MeSH secundário: Células HeLa
Seres Humanos
RNA Longo não Codificante
RNA Nuclear Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Long Noncoding); 0 (RNA, Small Nuclear); 0 (RNA-Binding Proteins); EC 2.7.11.- (Positive Transcriptional Elongation Factor B)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE


  10 / 3161 MEDLINE  
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[PMID]:28733144
[Au] Autor:Shi Y
[Ad] Endereço:Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China; Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Xihu District, Hangzhou 310064, Zhejiang Province, Province, China. Electronic address: shi-lab@tsinghua.edu.cn.
[Ti] Título:The Spliceosome: A Protein-Directed Metalloribozyme.
[So] Source:J Mol Biol;429(17):2640-2653, 2017 Aug 18.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pre-mRNA splicing is executed by the ribonucleoprotein machinery spliceosome. Nearly 40 years after the discovery of pre-mRNA splicing, the atomic structure of the spliceosome has finally come to light. Four distinct conformational states of the yeast spliceosome have been captured at atomic or near-atomic resolutions. Two catalytic metal ions at the active site are specifically coordinated by the U6 small nuclear RNA (snRNA) and catalyze both the branching reaction and the exon ligation. Of the three snRNAs in the fully assembled spliceosome, U5 and U6, along with 30 contiguous nucleotides of U2 at its 5'-end, remain structurally rigid throughout the splicing reaction. The rigidity of these RNA elements is safeguarded by Prp8 and 16 core protein components, which maintain the same overall conformation in all structurally characterized spliceosomes during the splicing reaction. Only the sequences downstream of nucleotide 30 of U2 snRNA are mobile; their movement, directed by the protein components, delivers the intron branch site into the close proximity of the 5'-splice site for the branching reaction. A set of additional structural rearrangement is required for exon ligation, and the lariat junction is moved out of the active site for recruitment of the 3'-splice site and 3'-exon. The spliceosome is proven to be a protein-directed metalloribozyme.
[Mh] Termos MeSH primário: Precursores de RNA/metabolismo
Processamento de RNA
Ribonucleoproteínas/química
Ribonucleoproteínas/metabolismo
Spliceossomos/química
Spliceossomos/metabolismo
[Mh] Termos MeSH secundário: Domínio Catalítico
Coenzimas/química
Coenzimas/metabolismo
Metais/química
Metais/metabolismo
Modelos Biológicos
Modelos Moleculares
Conformação Proteica
RNA Nuclear Pequeno/química
RNA Nuclear Pequeno/metabolismo
Saccharomyces cerevisiae/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Coenzymes); 0 (Metals); 0 (RNA Precursors); 0 (RNA, Small Nuclear); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170723
[St] Status:MEDLINE



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