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  1 / 6660 MEDLINE  
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[PMID]:29366779
[Au] Autor:Fukumura K; Inoue K; Mayeda A
[Ad] Endereço:Division of Gene Expression Mechanism, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake 470-1192, Aichi, Japan.
[Ti] Título:Splicing activator RNPS1 suppresses errors in pre-mRNA splicing: A key factor for mRNA quality control.
[So] Source:Biochem Biophys Res Commun;496(3):921-926, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human RNPS1 protein was first identified as a pre-mRNA splicing activator in vitro and RNPS1 regulates alternative splicing in cellulo. RNPS1 was also known as a peripheral factor of the exon junction complex (EJC). Here we show that cellular knockdown of RNPS1 induced a reduction of the wild-type aurora kinase B (AURKB) protein due to the induced aberrant pre-mRNA splicing events, indicating that the fidelity of AURKB pre-mRNA splicing was reduced. The major aberrant AURKB mRNA was derived from the upstream pseudo 5' and 3' splice sites in intron 5, which resulted in the production of the non-functional truncated AURKB protein. AURKB, is an essential mitotic factor, whose absence is known to cause multiple nuclei, and this multinucleation phenotype was recapitulated in RNPS1-knockdown cells. Importantly this RNPS1-knockdown phenotype was rescued by ectopic expression of AURKB, implying it is a major functional target of RNPS1. We found RNPS1 protein, not as a component of the EJC, binds directly to a specific element in the AURKB exon upstream of the authentic 5' splice site, and this binding is required for normal splicing. RNPS1-knockdown induces a parallel aberrant splicing pattern in a fully distinct pre-mRNA, MDM2, suggesting that RNPS1 is a global guardian of splicing fidelity. We conclude that RNPS1 is a key factor for the quality control of mRNAs that is essential for the phenotypes including cell division.
[Mh] Termos MeSH primário: Aurora Quinase B/genética
Genes Supressores
Precursores de RNA/genética
Processamento de RNA/genética
RNA Mensageiro/genética
Ribonucleoproteínas/genética
[Mh] Termos MeSH secundário: Células HeLa
Seres Humanos
Controle de Qualidade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (RNA Precursors); 0 (RNA, Messenger); 0 (RNPS1 protein, human); 0 (Ribonucleoproteins); EC 2.7.11.1 (AURKB protein, human); EC 2.7.11.1 (Aurora Kinase B)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


  2 / 6660 MEDLINE  
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[PMID]:29338026
[Au] Autor:Vanzyl EJ; Rick KRC; Blackmore AB; MacFarlane EM; McKay BC
[Ad] Endereço:Department of Biology, Carleton University, Ottawa ON, Canada.
[Ti] Título:Flow cytometric analysis identifies changes in S and M phases as novel cell cycle alterations induced by the splicing inhibitor isoginkgetin.
[So] Source:PLoS One;13(1):e0191178, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The spliceosome is a large ribonucleoprotein complex that catalyzes the removal of introns from RNA polymerase II-transcribed RNAs. Spliceosome assembly occurs in a stepwise manner through specific intermediates referred to as pre-spliceosome complexes E, A, B, B* and C. It has been reported that small molecule inhibitors of the spliceosome that target the SF3B1 protein component of complex A lead to the accumulation of cells in the G1 and G2/M phases of the cell cycle. Here we performed a comprehensive flow cytometry analysis of the effects of isoginkgetin (IGG), a natural compound that interferes with spliceosome assembly at a later step, complex B formation. We found that IGG slowed cell cycle progression in multiple phases of the cell cycle (G1, S and G2) but not M phase. This pattern was somewhat similar to but distinguishable from changes associated with an SF3B1 inhibitor, pladienolide B (PB). Both drugs led to a significant decrease in nascent DNA synthesis in S phase, indicative of an S phase arrest. However, IGG led to a much more prominent S phase arrest than PB while PB exhibited a more pronounced G1 arrest that decreased the proportion of cells in S phase as well. We also found that both drugs led to a comparable decrease in the proportion of cells in M phase. This work indicates that spliceosome inhibitors affect multiple phases of the cell cycle and that some of these effects vary in an agent-specific manner despite the fact that they target splicing at similar stages of spliceosome assembly.
[Mh] Termos MeSH primário: Biflavonoides/farmacologia
Divisão Celular/efeitos dos fármacos
Processamento de RNA/efeitos dos fármacos
Fase S/efeitos dos fármacos
[Mh] Termos MeSH secundário: Ciclo Celular/efeitos dos fármacos
Pontos de Checagem do Ciclo Celular/efeitos dos fármacos
Replicação do DNA/efeitos dos fármacos
Compostos de Epóxi/farmacologia
Citometria de Fluxo
Células HCT116
Seres Humanos
Macrolídeos/farmacologia
Precursores de RNA/metabolismo
Spliceossomos/efeitos dos fármacos
Spliceossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biflavonoids); 0 (Epoxy Compounds); 0 (Macrolides); 0 (RNA Precursors); 0 (isoginkgetin); 0 (pladienolide B)
[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:180117
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191178


  3 / 6660 MEDLINE  
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[PMID]:29330354
[Au] Autor:Bao P; Will CL; Urlaub H; Boon KL; Lührmann R
[Ad] Endereço:Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany.
[Ti] Título:The RES complex is required for efficient transformation of the precatalytic B spliceosome into an activated B complex.
[So] Source:Genes Dev;31(23-24):2416-2429, 2017 12 01.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The precise function of the trimeric retention and splicing (RES) complex in pre-mRNA splicing remains unclear. Here we dissected the role of RES during the assembly and activation of yeast spliceosomes. The efficiency of pre-mRNA splicing was significantly lower in the absence of the RES protein Snu17, and the recruitment of its binding partners, Pml1 (pre-mRNA leakage protein 1) and Bud13 (bud site selection protein 13), to the spliceosome was either abolished or substantially reduced. RES was not required for the assembly of spliceosomal B complexes, but its absence hindered efficient B complex formation. ΔRES spliceosomes were no longer strictly dependent on Prp2 activity for their catalytic activation, suggesting that they are structurally compromised. Addition of Prp2, Spp2, and UTP to affinity-purified ΔRES B or a mixture of B/B complexes formed on wild-type pre-mRNA led to their disassembly. However, no substantial disassembly was observed with ΔRES spliceosomes formed on a truncated pre-mRNA that allows Prp2 binding but blocks its activity. Thus, in the absence of RES, Prp2 appears to bind prematurely, leading to the disassembly of the ΔRES B complexes to which it binds. Our data suggest that Prp2 can dismantle B complexes with an aberrant protein composition, suggesting that it may proofread the spliceosome's RNP structure prior to activation.
[Mh] Termos MeSH primário: Processamento de RNA/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Spliceossomos/metabolismo
[Mh] Termos MeSH secundário: RNA Helicases DEAD-box/metabolismo
Multimerização Proteica/genética
Precursores de RNA/metabolismo
Ribonucleoproteína Nuclear Pequena U2/genética
Ribonucleoproteína Nuclear Pequena U2/metabolismo
Ribonucleoproteína Nuclear Pequena U4-U6/metabolismo
Spliceossomos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IST3 protein, S cerevisiae); 0 (RNA Precursors); 0 (Ribonucleoprotein, U2 Small Nuclear); 0 (Ribonucleoprotein, U4-U6 Small Nuclear); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (PRP2 protein, S cerevisiae); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180114
[St] Status:MEDLINE
[do] DOI:10.1101/gad.308163.117


  4 / 6660 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


  5 / 6660 MEDLINE  
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[PMID]:29269483
[Au] Autor:Huang H; Zhang J; Harvey SE; Hu X; Cheng C
[Ad] Endereço:Division of Hematology and Oncology, Department of Medicine, Robert H. Lurie Comprehensive Cancer Center, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611, USA.
[Ti] Título:RNA G-quadruplex secondary structure promotes alternative splicing via the RNA-binding protein hnRNPF.
[So] Source:Genes Dev;31(22):2296-2309, 2017 11 15.
[Is] ISSN:1549-5477
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is generally thought that splicing factors regulate alternative splicing through binding to RNA consensus sequences. In addition to these linear motifs, RNA secondary structure is emerging as an important layer in splicing regulation. Here we demonstrate that RNA elements with G-quadruplex-forming capacity promote exon inclusion. Destroying G-quadruplex-forming capacity while keeping G tracts intact abrogates exon inclusion. Analysis of RNA-binding protein footprints revealed that G quadruplexes are enriched in heterogeneous nuclear ribonucleoprotein F (hnRNPF)-binding sites and near hnRNPF-regulated alternatively spliced exons in the human transcriptome. Moreover, hnRNPF regulates an epithelial-mesenchymal transition (EMT)-associated CD44 isoform switch in a G-quadruplex-dependent manner, which results in inhibition of EMT. Mining breast cancer TCGA (The Cancer Genome Atlas) data sets, we demonstrate that hnRNPF negatively correlates with an EMT gene signature and positively correlates with patient survival. These data suggest a critical role for RNA G quadruplexes in regulating alternative splicing. Modulation of G-quadruplex structural integrity may control cellular processes important for tumor progression.
[Mh] Termos MeSH primário: Processamento Alternativo
Quadruplex G
Ribonucleoproteínas Nucleares Heterogêneas Grupo F-H/metabolismo
RNA/química
[Mh] Termos MeSH secundário: Neoplasias da Mama/metabolismo
Neoplasias da Mama/mortalidade
Linhagem Celular
Transição Epitelial-Mesenquimal
Éxons
Feminino
Seres Humanos
Receptores de Hialuronatos/genética
Invasividade Neoplásica
RNA/metabolismo
Precursores de RNA/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Heterogeneous-Nuclear Ribonucleoprotein Group F-H); 0 (Hyaluronan Receptors); 0 (RNA Precursors); 63231-63-0 (RNA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.1101/gad.305862.117


  6 / 6660 MEDLINE  
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[PMID]:29216001
[Au] Autor:Demirci MDS; Toprak M; Allmer J
[Ad] Endereço:.
[Ti] Título:A Machine Learning Approach for MicroRNA Precursor Prediction in Retro-transcribing Virus Genomes.
[So] Source:J Integr Bioinform;13(5):3-10, 2016 Dec 01.
[Is] ISSN:1613-4516
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Identification of microRNA (miRNA) precursors has seen increased efforts in recent years. The difficulty in experimental detection of pre-miRNAs increased the usage of computational approaches. Most of these approaches rely on machine learning especially classification. In order to achieve successful classification, many parameters need to be considered such as data quality, choice of classifier settings, and feature selection. For the latter one, we developed a distributed genetic algorithm on HTCondor to perform feature selection. Moreover, we employed two widely used classification algorithms libSVM and random forest with different settings to analyze the influence on the overall classification performance. In this study we analyzed 5 human retro virus genomes; Human endogenous retrovirus K113, Hepatitis B virus (strain ayw), Human T lymphotropic virus 1, Human T lymphotropic virus 2, Human immunodeficiency virus 2, and Human immunodeficiency virus 1. We then predicted pre-miRNAs by using the information from known virus and human pre-miRNAs. Our results indicate that these viruses produce novel unknown miRNA precursors which warrant further experimental validation.
[Mh] Termos MeSH primário: Biologia Computacional
Genoma Viral
Aprendizado de Máquina
MicroRNAs/genética
Precursores de RNA/genética
[Mh] Termos MeSH secundário: Algoritmos
Simulação por Computador
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MicroRNAs); 0 (RNA Precursors)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE


  7 / 6660 MEDLINE  
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[PMID]:29244186
[Au] Autor:Nanan KK; Ocheltree C; Sturgill D; Mandler MD; Prigge M; Varma G; Oberdoerffer S
[Ad] Endereço:Laboratory of Receptor Biology and Gene Expression, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
[Ti] Título:Independence between pre-mRNA splicing and DNA methylation in an isogenic minigene resource.
[So] Source:Nucleic Acids Res;45(22):12780-12797, 2017 Dec 15.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Actively transcribed genes adopt a unique chromatin environment with characteristic patterns of enrichment. Within gene bodies, H3K36me3 and cytosine DNA methylation are elevated at exons of spliced genes and have been implicated in the regulation of pre-mRNA splicing. H3K36me3 is further responsive to splicing, wherein splicing inhibition led to a redistribution and general reduction over gene bodies. In contrast, little is known of the mechanisms supporting elevated DNA methylation at actively spliced genic locations. Recent evidence associating the de novo DNA methyltransferase Dnmt3b with H3K36me3-rich chromatin raises the possibility that genic DNA methylation is influenced by splicing-associated H3K36me3. Here, we report the generation of an isogenic resource to test the direct impact of splicing on chromatin. A panel of minigenes of varying splicing potential were integrated into a single FRT site for inducible expression. Profiling of H3K36me3 confirmed the established relationship to splicing, wherein levels were directly correlated with splicing efficiency. In contrast, DNA methylation was equivalently detected across the minigene panel, irrespective of splicing and H3K36me3 status. In addition to revealing a degree of independence between genic H3K36me3 and DNA methylation, these findings highlight the generated minigene panel as a flexible platform for the query of splicing-dependent chromatin modifications.
[Mh] Termos MeSH primário: Metilação de DNA
Éxons/genética
Precursores de RNA/genética
Processamento de RNA
[Mh] Termos MeSH secundário: Animais
Cromatina/genética
Cromatina/metabolismo
DNA (Citosina-5-)-Metiltransferases/metabolismo
Regulação da Expressão Gênica
Células HEK293
Histonas/metabolismo
Seres Humanos
Lisina/metabolismo
Metilação
Camundongos
Modelos Genéticos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 0 (RNA Precursors); EC 2.1.1.37 (DNA (Cytosine-5-)-Methyltransferases); EC 2.1.1.37 (DNA methyltransferase 3B); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx900


  8 / 6660 MEDLINE  
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[PMID]:29174924
[Au] Autor:Liang D; Tatomer DC; Luo Z; Wu H; Yang L; Chen LL; Cherry S; Wilusz JE
[Ad] Endereço:Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA.
[Ti] Título:The Output of Protein-Coding Genes Shifts to Circular RNAs When the Pre-mRNA Processing Machinery Is Limiting.
[So] Source:Mol Cell;68(5):940-954.e3, 2017 Dec 07.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many eukaryotic genes generate linear mRNAs and circular RNAs, but it is largely unknown how the ratio of linear to circular RNA is controlled or modulated. Using RNAi screening in Drosophila cells, we identify many core spliceosome and transcription termination factors that control the RNA outputs of reporter and endogenous genes. When spliceosome components were depleted or inhibited pharmacologically, the steady-state levels of circular RNAs increased while expression of their associated linear mRNAs concomitantly decreased. Upon inhibiting RNA polymerase II termination via depletion of the cleavage/polyadenylation machinery, circular RNA levels were similarly increased. This is because readthrough transcripts now extend into downstream genes and are subjected to backsplicing. In total, these results demonstrate that inhibition or slowing of canonical pre-mRNA processing events shifts the steady-state output of protein-coding genes toward circular RNAs. This is in part because nascent RNAs become directed into alternative pathways that lead to circular RNA production.
[Mh] Termos MeSH primário: Proteínas de Drosophila/genética
Drosophila melanogaster/genética
Precursores de RNA/biossíntese
Processamento de RNA
RNA Mensageiro/biossíntese
RNA/biossíntese
Spliceossomos/genética
Transcrição Genética
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Proteínas de Drosophila/biossíntese
Drosophila melanogaster/metabolismo
Lacase/biossíntese
Lacase/genética
RNA/genética
Interferência de RNA
RNA Polimerase II/metabolismo
Precursores de RNA/genética
Fatores de Processamento de RNA/genética
Fatores de Processamento de RNA/metabolismo
Estabilidade de RNA
RNA Mensageiro/genética
Ribonucleoproteínas Nucleolares Pequenas/genética
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
Spliceossomos/metabolismo
Terminação da Transcrição Genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (RNA Precursors); 0 (RNA Splicing Factors); 0 (RNA, Messenger); 0 (RNA, circular); 0 (Ribonucleoproteins, Small Nucleolar); 0 (ribonucleoprotein, U3 small nucleolar); 63231-63-0 (RNA); EC 1.10.3.2 (Laccase); EC 2.7.7.- (RNA Polymerase II)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  9 / 6660 MEDLINE  
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[PMID]:28744787
[Au] Autor:Krchnáková Z; Krajcovic J; Vesteg M
[Ad] Endereço:Department of RNA Biology, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
[Ti] Título:On the Possibility of an Early Evolutionary Origin for the Spliced Leader Trans-Splicing.
[So] Source:J Mol Evol;85(1-2):37-45, 2017 Aug.
[Is] ISSN:1432-1432
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Trans-splicing is a process by which 5'- and 3'-ends of two pre-RNA molecules transcribed from different sites of the genome can be joined together to form a single RNA molecule. The spliced leader (SL) trans-splicing is mediated by the spliceosome and it allows the replacement of 5'-end of pre-mRNA by 5'(SL)-end of SL-RNA. This form of splicing has been observed in many phylogenetically unrelated eukaryotes. Either the SL trans-splicing (SLTS) originated in the last eukaryotic common ancestor (LECA) (or even earlier) and it was lost in most eukaryotic lineages, or this mechanism of RNA processing evolved several times independently in various unrelated eukaryotic taxa. The bioinformatic comparisons of SL-RNAs from various eukaryotic taxonomic groups have revealed the similarities of secondary structures of most SL-RNAs and a relative conservation of their splice sites (SSs) and Sm-binding sites (SmBSs). We propose that such structural and functional similarities of SL-RNAs are unlikely to have evolved repeatedly many times. Hence, we favor the scenario of an early evolutionary origin for the SLTS and multiple losses of SL-RNAs in various eukaryotic lineages.
[Mh] Termos MeSH primário: Eucariotos/genética
Evolução Molecular
RNA Líder para Processamento/genética
Trans-Splicing
[Mh] Termos MeSH secundário: Eucariotos/metabolismo
Filogenia
Precursores de RNA/metabolismo
RNA Líder para Processamento/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (RNA Precursors); 0 (RNA, Spliced Leader)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171207
[Lr] Data última revisão:
171207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1007/s00239-017-9803-y


  10 / 6660 MEDLINE  
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[PMID]:29020104
[Au] Autor:Aik WS; Lin MH; Tan D; Tripathy A; Marzluff WF; Dominski Z; Chou CY; Tong L
[Ad] Endereço:Department of Biological Sciences, Columbia University, New York, New York, United States of America.
[Ti] Título:The N-terminal domains of FLASH and Lsm11 form a 2:1 heterotrimer for histone pre-mRNA 3'-end processing.
[So] Source:PLoS One;12(10):e0186034, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Unlike canonical pre-mRNAs, animal replication-dependent histone pre-mRNAs lack introns and are processed at the 3'-end by a mechanism distinct from cleavage and polyadenylation. They have a 3' stem loop and histone downstream element (HDE) that are recognized by stem-loop binding protein (SLBP) and U7 snRNP, respectively. The N-terminal domain (NTD) of Lsm11, a component of U7 snRNP, interacts with FLASH NTD and these two proteins recruit the histone cleavage complex containing the CPSF-73 endonuclease for the cleavage reaction. Here, we determined crystal structures of FLASH NTD and found that it forms a coiled-coil dimer. Using solution light scattering, we characterized the stoichiometry of the FLASH NTD-Lsm11 NTD complex and found that it is a 2:1 heterotrimer, which is supported by observations from analytical ultracentrifugation and crosslinking.
[Mh] Termos MeSH primário: Proteínas de Transporte/química
Proteínas de Transporte/metabolismo
Histonas/metabolismo
Multimerização Proteica
Precursores de RNA/metabolismo
Processamento Pós-Transcricional do RNA
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Fenômenos Biofísicos
Cromatografia em Gel
Cristalografia por Raios X
Cisteína/genética
Luz
Mutação/genética
Ligação Proteica
Domínios Proteicos
Estrutura Secundária de Proteína
Espalhamento de Radiação
Alinhamento de Sequência
Ultracentrifugação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Histones); 0 (RNA Precursors); 0 (RNA-Binding Proteins); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171012
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186034



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