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Pesquisa : D12.776.157.725.500.875 [Categoria DeCS]
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[PMID]:27773687
[Au] Autor:Ulrich AKC; Seeger M; Schütze T; Bartlick N; Wahl MC
[Ad] Endereço:Laboratory of Structural Biochemistry, Freie Universität Berlin, Takustraße 6, 14195 Berlin, Germany.
[Ti] Título:Scaffolding in the Spliceosome via Single α Helices.
[So] Source:Structure;24(11):1972-1983, 2016 11 01.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The spliceosomal B complex-specific protein Prp38 forms a complex with the intrinsically unstructured proteins MFAP1 and Snu23. Our binding and crystal structure analyses show that MFAP1 and Snu23 contact Prp38 via ER/K motif-stabilized single α helices, which have previously been recognized only as rigid connectors or force springs between protein domains. A variant of the Prp38-binding single α helix of MFAP1, in which ER/K motifs not involved in Prp38 binding were mutated, was less α-helical in isolation and showed a reduced Prp38 affinity, with opposing tendencies in interaction enthalpy and entropy. Our results indicate that the strengths of single α helix-based interactions can be tuned by the degree of helix stabilization in the unbound state. MFAP1, Snu23, and several other spliceosomal proteins contain multiple regions that likely form single α helices via which they might tether several binding partners and act as intermittent scaffolds that facilitate remodeling steps during assembly of an active spliceosome.
[Mh] Termos MeSH primário: Proteínas Contráteis/química
Proteínas da Matriz Extracelular/química
Fatores de Processamento de RNA/química
Ribonucleoproteínas Nucleares Pequenas/química
Spliceossomos/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Dicroísmo Circular
Cristalografia por Raios X
Seres Humanos
Modelos Moleculares
Ligação Proteica
Estrutura Secundária de Proteína
Termodinâmica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Contractile Proteins); 0 (Extracellular Matrix Proteins); 0 (RNA Splicing Factors); 0 (Ribonucleoproteins, Small Nuclear); 0 (microfibrillar protein)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171230
[Lr] Data última revisão:
171230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161103
[St] Status:MEDLINE


  2 / 2689 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


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[PMID]:28781166
[Au] Autor:Bertram K; Agafonov DE; Dybkov O; Haselbach D; Leelaram MN; Will CL; Urlaub H; Kastner B; Lührmann R; Stark H
[Ad] Endereço:Department of Structural Dynamics, MPI for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
[Ti] Título:Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.
[So] Source:Cell;170(4):701-713.e11, 2017 Aug 10.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Little is known about the spliceosome's structure before its extensive remodeling into a catalytically active complex. Here, we report a 3D cryo-EM structure of a pre-catalytic human spliceosomal B complex. The U2 snRNP-containing head domain is connected to the B complex main body via three main bridges. U4/U6.U5 tri-snRNP proteins, which are located in the main body, undergo significant rearrangements during tri-snRNP integration into the B complex. These include formation of a partially closed Prp8 conformation that creates, together with Dim1, a 5' splice site (ss) binding pocket, displacement of Sad1, and rearrangement of Brr2 such that it contacts its U4/U6 substrate and is poised for the subsequent spliceosome activation step. The molecular organization of several B-specific proteins suggests that they are involved in negatively regulating Brr2, positioning the U6/5'ss helix, and stabilizing the B complex structure. Our results indicate significant differences between the early activation phase of human and yeast spliceosomes.
[Mh] Termos MeSH primário: Spliceossomos/química
[Mh] Termos MeSH secundário: Núcleo Celular/química
Microscopia Crioeletrônica
Células HeLa
Seres Humanos
Modelos Moleculares
Proteínas de Ligação a RNA/química
Ribonucleoproteínas Nucleares Pequenas/química
Saccharomyces cerevisiae/química
Spliceossomos/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA-Binding Proteins); 0 (Ribonucleoproteins, Small Nuclear)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170808
[St] Status:MEDLINE


  4 / 2689 MEDLINE  
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[PMID]:28751196
[Au] Autor:Ito M; Iwatani M; Yamamoto T; Tanaka T; Kawamoto T; Morishita D; Nakanishi A; Maezaki H
[Ad] Endereço:Pharmaceutical Research Division, Takeda Pharmaceutical Company Limited, 26-1, Muraoka-Higashi 2-chome, Fujisawa, Kanagawa 251-8555, Japan. Electronic address: masahiro.ito@takeda.com.
[Ti] Título:Discovery of spiro[indole-3,2'-pyrrolidin]-2(1H)-one based inhibitors targeting Brr2, a core component of the U5 snRNP.
[So] Source:Bioorg Med Chem;25(17):4753-4767, 2017 Sep 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bad response to refrigeration 2 (Brr2) is a member of the Ski2-like RNA helicases, and an essential component of the U5 small nuclear ribonucleoprotein (snRNP). A particularly important role of Brr2 is the ATP-dependent unwinding of the U4/U6 RNA duplex, which is a critical step in spliceosomal activation. Despite its biological importance, selective inhibitor for Brr2 had not been reported until our recent report. Here, we describe novel and structurally distinct spiro[indole-3,2'-pyrrolidin]-2(1H)-one based Brr2 inhibitors with superior activity to the previously reported 4,6-dihydropyrido[4,3-d]pyrimidine-2,7(1H,3H)-dione series. Using an RNA dependent ATPase assay as a guide, high-throughput screening, hit validation by structure-activity relationship (SAR) study, and subsequent chemical optimization to increase the ATPase inhibitory activity were performed. Thereafter, selectivity and helicase inhibitory activity of optimized compounds were confirmed. In the course of the study, compounds were synthesized using a three-component reaction, which accelerated the optimization process. All these efforts finally culminated in the discovery of the potent and selective Brr2 inhibitors (32a and 33a) exhibiting helicase inhibitory activity at submicromolar concentrations. Thus, compounds 32a and 33a could be valuable molecular probes to study the functions of Brr2 and molecular machinery of RNA splicing.
[Mh] Termos MeSH primário: Ribonucleoproteínas Nucleares Pequenas/antagonistas & inibidores
Compostos de Espiro/química
[Mh] Termos MeSH secundário: Seres Humanos
Indóis/química
Concentração Inibidora 50
Ligação Proteica
RNA Helicases/antagonistas & inibidores
RNA Helicases/metabolismo
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Ribonucleoproteínas Nucleares Pequenas/genética
Ribonucleoproteínas Nucleares Pequenas/metabolismo
Compostos de Espiro/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Indoles); 0 (Recombinant Proteins); 0 (Ribonucleoproteins, Small Nuclear); 0 (SNRNP200 protein, human); 0 (Spiro Compounds); EC 3.6.4.13 (RNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170729
[St] Status:MEDLINE


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[PMID]:28666385
[Au] Autor:Gopanenko AV; Malygin AA; Tupikin AE; Laktionov PP; Kabilov MR; Karpova GG
[Ad] Endereço:Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk 630090, Russia.
[Ti] Título:Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA.
[So] Source:Nucleic Acids Res;45(15):9121-9137, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ribosomal proteins are involved in many cellular processes through interactions with various RNAs. Here, applying the photoactivatable-ribonucleoside-enhanced cross-linking and immunoprecipitation approach to HEK293 cells overproducing ribosomal protein (rp) eS1, we determined the products of RNU5A-1 and RNU11 genes encoding U5 and U11 snRNAs as the RNA partners of ribosome-unbound rp eS1. U11 pre-snRNA-associated rp eS1 was revealed in the cytoplasm and nucleus where rp eS1-bound U11/U12 di-snRNP was also found. Utilizing recombinant rp eS1 and 4-thiouridine-containing U11 snRNA transcript, we identified an N-terminal peptide contacting the U-rich sequence in the Sm site-containing RNA region. We also showed that the rp eS1 binding site on U11 snRNA is located in the cleft between stem-loops I and III and that its structure mimics the respective site on the 18S rRNA. It was found that cell depletion of rp eS1 leads to a decrease in the splicing efficiency of minor introns and to an increase in the level of U11 pre-snRNA with the unprocessed 3' terminus. Our findings demonstrate the engagement of human rp eS1 in events related to the U11 snRNA processing and to minor-class splicing. Contacts of rp eS1 with U5 snRNA in the minor pre-catalytic spliceosome are discussed.
[Mh] Termos MeSH primário: Biossíntese de Proteínas
Processamento de RNA
RNA Ribossômico 18S/genética
RNA Nuclear Pequeno/química
Ribonucleoproteínas Nucleares Pequenas/genética
Proteínas Ribossômicas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Sequência de Bases
Escherichia coli/genética
Escherichia coli/metabolismo
Células HEK293
Seres Humanos
Íntrons
Modelos Moleculares
Conformação de Ácido Nucleico
Conformação Proteica em alfa-Hélice
Domínios e Motivos de Interação entre Proteínas
RNA Ribossômico 18S/metabolismo
RNA Nuclear Pequeno/genética
RNA Nuclear Pequeno/metabolismo
Ribonucleoproteínas Nucleares Pequenas/metabolismo
Proteínas Ribossômicas/genética
Proteínas Ribossômicas/metabolismo
Ribossomos/genética
Ribossomos/metabolismo
Spliceossomos/genética
Spliceossomos/metabolismo
Tiouridina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Ribosomal, 18S); 0 (RNA, Small Nuclear); 0 (RPS3A protein, human); 0 (Ribonucleoproteins, Small Nuclear); 0 (Ribosomal Proteins); 0 (U11 small nuclear ribonucleoprotein, human); 13957-31-8 (Thiouridine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx559


  6 / 2689 MEDLINE  
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[PMID]:28637748
[Au] Autor:Prusty AB; Meduri R; Prusty BK; Vanselow J; Schlosser A; Fischer U
[Ad] Endereço:Department of Biochemistry, Biocenter, University of Würzburg, Am Hubland, Würzburg, Germany.
[Ti] Título:Impaired spliceosomal UsnRNP assembly leads to Sm mRNA down-regulation and Sm protein degradation.
[So] Source:J Cell Biol;216(8):2391-2407, 2017 Aug 07.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Specialized assembly factors facilitate the formation of many macromolecular complexes in vivo. The formation of Sm core structures of spliceosomal U-rich small nuclear ribonucleoprotein particles (UsnRNPs) requires assembly factors united in protein arginine methyltransferase 5 (PRMT5) and survival motor neuron (SMN) complexes. We demonstrate that perturbations of this assembly machinery trigger complex cellular responses that prevent aggregation of unassembled Sm proteins. Inactivation of the SMN complex results in the initial tailback of Sm proteins on the PRMT5 complex, followed by down-regulation of their encoding mRNAs. In contrast, reduction of pICln, a PRMT5 complex subunit, leads to the retention of newly synthesized Sm proteins on ribosomes and their subsequent lysosomal degradation. Overexpression of Sm proteins under these conditions results in a surplus of Sm proteins over pICln, promoting their aggregation. Our studies identify an elaborate safeguarding system that prevents individual Sm proteins from aggregating, contributing to cellular UsnRNP homeostasis.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
RNA Mensageiro/metabolismo
Ribonucleoproteínas Nucleares Pequenas/metabolismo
Spliceossomos/metabolismo
[Mh] Termos MeSH secundário: Autofagia
Regulação para Baixo
Células HeLa
Seres Humanos
Canais Iônicos/genética
Canais Iônicos/metabolismo
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Fosforilação
Agregados Proteicos
Estabilidade Proteica
Proteína-Arginina N-Metiltransferases/genética
Proteína-Arginina N-Metiltransferases/metabolismo
Proteólise
Interferência de RNA
Estabilidade de RNA
RNA Mensageiro/genética
Ribonucleoproteínas Nucleares Pequenas/genética
Proteínas do Complexo SMN/genética
Proteínas do Complexo SMN/metabolismo
Spliceossomos/genética
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CLNS1A protein, human); 0 (Ion Channels); 0 (Molecular Chaperones); 0 (Protein Aggregates); 0 (RNA, Messenger); 0 (Ribonucleoproteins, Small Nuclear); 0 (SMN Complex Proteins); EC 2.1.1.319 (PRMT5 protein, human); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201611108


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[PMID]:28582530
[Au] Autor:Philippe L; Pandarakalam GC; Fasimoye R; Harrison N; Connolly B; Pettitt J; Müller B
[Ad] Endereço:School of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Institute of Medical Sciences, Foresterhill, Aberdeen AB25 2ZD, UK.
[Ti] Título:An in vivo genetic screen for genes involved in spliced leader trans-splicing indicates a crucial role for continuous de novo spliced leader RNP assembly.
[So] Source:Nucleic Acids Res;45(14):8474-8483, 2017 Aug 21.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Spliced leader (SL) trans-splicing is a critical element of gene expression in a number of eukaryotic groups. This process is arguably best understood in nematodes, where biochemical and molecular studies in Caenorhabditis elegans and Ascaris suum have identified key steps and factors involved. Despite this, the precise details of SL trans-splicing have yet to be elucidated. In part, this is because the systematic identification of the molecules involved has not previously been possible due to the lack of a specific phenotype associated with defects in this process. We present here a novel GFP-based reporter assay that can monitor SL1 trans-splicing in living C. elegans. Using this assay, we have identified mutants in sna-1 that are defective in SL trans-splicing, and demonstrate that reducing function of SNA-1, SNA-2 and SUT-1, proteins that associate with SL1 RNA and related SmY RNAs, impairs SL trans-splicing. We further demonstrate that the Sm proteins and pICln, SMN and Gemin5, which are involved in small nuclear ribonucleoprotein assembly, have an important role in SL trans-splicing. Taken together these results provide the first in vivo evidence for proteins involved in SL trans-splicing, and indicate that continuous replacement of SL ribonucleoproteins consumed during trans-splicing reactions is essential for effective trans-splicing.
[Mh] Termos MeSH primário: Proteínas de Helminto/genética
RNA de Helmintos/genética
RNA Líder para Processamento/genética
Ribonucleoproteínas/genética
Trans-Splicing
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Sequência de Bases
Caenorhabditis elegans/genética
Caenorhabditis elegans/metabolismo
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Proteínas de Helminto/metabolismo
Microscopia de Fluorescência
Interferência de RNA
Precursores de RNA/genética
Precursores de RNA/metabolismo
RNA de Helmintos/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Líder para Processamento/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Ribonucleoproteínas/metabolismo
Ribonucleoproteínas Nucleares Pequenas/genética
Ribonucleoproteínas Nucleares Pequenas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Helminth Proteins); 0 (RNA Precursors); 0 (RNA, Helminth); 0 (RNA, Messenger); 0 (RNA, Spliced Leader); 0 (Ribonucleoproteins); 0 (Ribonucleoproteins, Small Nuclear); 147336-22-9 (Green Fluorescent Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx500


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[PMID]:28570645
[Au] Autor:Li W
[Ad] Endereço:Medical College, Shantou University, Shantou City, Guangdong Province, China.
[Ti] Título:How do SMA-linked mutations of SMN1 lead to structural/functional deficiency of the SMA protein?
[So] Source:PLoS One;12(6):e0178519, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Spinal muscular atrophy (SMA) is an autosomal recessive neuromuscular disease with dysfunctional α-motor neurons in the anterior horn of the spinal cord. SMA is caused by loss (∼95% of SMA cases) or mutation (∼5% of SMA cases) of the survival motor neuron 1 gene SMN1. As the product of SMN1, SMN is a component of the SMN complex, and is also involved in the biosynthesis of the small nuclear ribonucleoproteins (snRNPs), which play critical roles in pre-mRNA splicing in the pathogenesis of SMA. To investigate how SMA-linked mutations of SMN1 lead to structural/functional deficiency of SMN, a set of computational analysis of SMN-related structures were conducted and are described in this article. Of extraordinary interest, the structural analysis highlights three SMN residues (Asp44, Glu134 and Gln136) with SMA-linked missense mutations, which cause disruptions of electrostatic interactions for Asp44, Glu134 and Gln136, and result in three functionally deficient SMA-linked SMN mutants, Asp44Val, Glu134Lys and Gln136Glu. From the computational analysis, it is also possible that SMN's Lys45 and Asp36 act as two electrostatic clips at the SMN-Gemin2 complex structure interface.
[Mh] Termos MeSH primário: Atrofia Muscular Espinal/genética
Mutação
Proteína 1 de Sobrevivência do Neurônio Motor/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Seres Humanos
Ribonucleoproteínas Nucleares Pequenas/metabolismo
Eletricidade Estática
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ribonucleoproteins, Small Nuclear); 0 (SMN1 protein, human); 0 (Survival of Motor Neuron 1 Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170602
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178519


  9 / 2689 MEDLINE  
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[PMID]:28549066
[Au] Autor:Verbeeren J; Verma B; Niemelä EH; Yap K; Makeyev EV; Frilander MJ
[Ad] Endereço:Institute of Biotechnology, FI-00014 University of Helsinki, Helsinki, Finland.
[Ti] Título:Alternative exon definition events control the choice between nuclear retention and cytoplasmic export of U11/U12-65K mRNA.
[So] Source:PLoS Genet;13(5):e1006824, 2017 May.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular homeostasis of the minor spliceosome is regulated by a negative feed-back loop that targets U11-48K and U11/U12-65K mRNAs encoding essential components of the U12-type intron-specific U11/U12 di-snRNP. This involves interaction of the U11 snRNP with an evolutionarily conserved splicing enhancer giving rise to unproductive mRNA isoforms. In the case of U11/U12-65K, this mechanism controls the length of the 3' untranslated region (3'UTR). We show that this process is dynamically regulated in developing neurons and some other cell types, and involves a binary switch between translation-competent mRNAs with a short 3'UTR to non-productive isoforms with a long 3'UTR that are retained in the nucleus or/and spliced to the downstream amylase locus. Importantly, the choice between these alternatives is determined by alternative terminal exon definition events regulated by conserved U12- and U2-type 5' splice sites as well as sequence signals used for pre-mRNA cleavage and polyadenylation. We additionally show that U11 snRNP binding to the U11/U12-65K mRNA species with a long 3'UTR is required for their nuclear retention. Together, our studies uncover an intricate molecular circuitry regulating the abundance of a key spliceosomal protein and shed new light on the mechanisms limiting the export of non-productively spliced mRNAs from the nucleus to the cytoplasm.
[Mh] Termos MeSH primário: Processamento Alternativo
Núcleo Celular/metabolismo
Éxons
Ribonucleoproteínas Nucleares Pequenas/genética
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Animais
Células CHO
Células Cultivadas
Cricetinae
Cricetulus
Citoplasma/metabolismo
Células HEK293
Células HeLa
Seres Humanos
Camundongos
Ligação Proteica
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ribonucleoproteínas Nucleares Pequenas/metabolismo
Spliceossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Ribonucleoproteins, Small Nuclear); 0 (U11-U12 small nuclear ribonucleoprotein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006824


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[PMID]:28505348
[Au] Autor:Rothé B; Manival X; Rolland N; Charron C; Senty-Ségault V; Branlant C; Charpentier B
[Ad] Endereço:Ingénierie Moléculaire et Physiopathologie Articulaire (IMoPA), UMR 7365 CNRS Université de Lorraine, Biopôle, Campus Biologie Santé, 9 avenue de la forêt de Haye, BP 20199, 54505 VandÅ“uvre-lès-Nancy, France.
[Ti] Título:Implication of the box C/D snoRNP assembly factor Rsa1p in U3 snoRNP assembly.
[So] Source:Nucleic Acids Res;45(12):7455-7473, 2017 Jul 07.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The U3 box C/D snoRNA is one key element of 90S pre-ribosome. It contains a 5΄ domain pairing with pre-rRNA and the U3B/C and U3C΄/D motifs for U3 packaging into a unique small nucleolar ribonucleoprotein particle (snoRNP). The RNA-binding protein Snu13/SNU13 nucleates on U3B/C the assembly of box C/D proteins Nop1p/FBL and Nop56p/NOP56, and the U3-specific protein Rrp9p/U3-55K. Snu13p/SNU13 has a much lower affinity for U3C΄/D but nevertheless forms on this motif an RNP with box C/D proteins Nop1p/FBL and Nop58p/NOP58. In this study, we characterized the influence of the RNP assembly protein Rsa1 in the early steps of U3 snoRNP biogenesis in yeast and we propose a refined model of U3 snoRNP biogenesis. While recombinant Snu13p enhances the binding of Rrp9p to U3B/C, we observed that Rsa1p has no effect on this activity but forms with Snu13p and Rrp9p a U3B/C pre-RNP. In contrast, we found that Rsa1p enhances Snu13p binding on U3C΄/D. RNA footprinting experiments indicate that this positive effect most likely occurs by direct contacts of Rsa1p with the U3 snoRNA 5΄ domain. In light of the recent U3 snoRNP cryo-EM structures, our data suggest that Rsa1p has a dual role by also preventing formation of a pre-mature functional U3 RNP.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica
Precursores de RNA/genética
RNA Nucleolar Pequeno/genética
Ribonucleoproteínas Nucleares Pequenas/genética
Ribonucleoproteínas Nucleolares Pequenas/genética
Proteínas Ribossômicas/genética
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Sítios de Ligação
Proteínas Nucleares/genética
Proteínas Nucleares/metabolismo
Conformação de Ácido Nucleico
Ligação Proteica
Precursores de RNA/metabolismo
RNA Nucleolar Pequeno/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Ribonucleoproteínas Nucleares Pequenas/metabolismo
Ribonucleoproteínas Nucleolares Pequenas/metabolismo
Proteínas Ribossômicas/metabolismo
Ribossomos/genética
Ribossomos/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NOP1 protein, S cerevisiae); 0 (NOP56 protein, S cerevisiae); 0 (Nuclear Proteins); 0 (RNA Precursors); 0 (RNA, Small Nucleolar); 0 (RNA, U3 small nucleolar); 0 (RSA1 protein, S cerevisiae); 0 (Recombinant Proteins); 0 (Ribonucleoproteins, Small Nuclear); 0 (Ribonucleoproteins, Small Nucleolar); 0 (Ribosomal Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Snu13 protein, S cerevisiae); 0 (ribonucleoprotein, U3 small nucleolar)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170516
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx424



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