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[PMID]:27095199
[Au] Autor:Flamand MN; Wu E; Vashisht A; Jannot G; Keiper BD; Simard MJ; Wohlschlegel J; Duchaine TF
[Ad] Endereço:Department of Biochemistry, McGill University, Montreal, QC H3A 1A3, Canada Goodman Cancer Research Center, McGill University, Montreal, QC H3A 1A3, Canada.
[Ti] Título:Poly(A)-binding proteins are required for microRNA-mediated silencing and to promote target deadenylation in C. elegans.
[So] Source:Nucleic Acids Res;44(12):5924-35, 2016 Jul 08.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cytoplasmic poly(A)-binding proteins (PABPs) link mRNA 3' termini to translation initiation factors, but they also play key roles in mRNA regulation and decay. Reports from mice, zebrafish and Drosophila further involved PABPs in microRNA (miRNA)-mediated silencing, but through seemingly distinct mechanisms. Here, we implicate the two Caenorhabditis elegans PABPs (PAB-1 and PAB-2) in miRNA-mediated silencing, and elucidate their mechanisms of action using concerted genetics, protein interaction analyses, and cell-free assays. We find that C. elegans PABPs are required for miRNA-mediated silencing in embryonic and larval developmental stages, where they act through a multi-faceted mechanism. Depletion of PAB-1 and PAB-2 results in loss of both poly(A)-dependent and -independent translational silencing. PABPs accelerate miRNA-mediated deadenylation, but this contribution can be modulated by 3'UTR sequences. While greater distances with the poly(A) tail exacerbate dependency on PABP for deadenylation, more potent miRNA-binding sites partially suppress this effect. Our results refine the roles of PABPs in miRNA-mediated silencing and support a model wherein they enable miRNA-binding sites by looping the 3'UTR poly(A) tail to the bound miRISC and deadenylase.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/genética
Caenorhabditis elegans/genética
Larva/genética
MicroRNAs/genética
Poli A/genética
Proteína II de Ligação a Poli(A)/genética
Proteína I de Ligação a Poli(A)/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Monofosfato de Adenosina/metabolismo
Animais
Sítios de Ligação
Caenorhabditis elegans/crescimento & desenvolvimento
Caenorhabditis elegans/metabolismo
Proteínas de Caenorhabditis elegans/metabolismo
Embrião não Mamífero
Inativação Gênica
Larva/crescimento & desenvolvimento
Larva/metabolismo
MicroRNAs/metabolismo
Poli A/metabolismo
Proteína I de Ligação a Poli(A)/metabolismo
Proteína II de Ligação a Poli(A)/metabolismo
Ligação Proteica
Biossíntese de Proteínas
Complexo de Inativação Induzido por RNA/genética
Complexo de Inativação Induzido por RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Caenorhabditis elegans Proteins); 0 (MicroRNAs); 0 (Poly(A)-Binding Protein I); 0 (Poly(A)-Binding Protein II); 0 (RNA-Induced Silencing Complex); 24937-83-5 (Poly A); 415SHH325A (Adenosine Monophosphate)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160421
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw276


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[PMID]:25720531
[Au] Autor:van Zalen S; Lombardi AA; Jeschke GR; Hexner EO; Russell JE
[Ad] Endereço:Department of Medicine (Hematology-Oncology), Perelman School of Medicine, University of Pennsylvania, 3400 Spruce Street, Philadelphia, PA 19104, USA.
[Ti] Título:AUF-1 and YB-1 independently regulate ß-globin mRNA in developing erythroid cells through interactions with poly(A)-binding protein.
[So] Source:Mech Dev;136:40-52, 2015 May.
[Is] ISSN:1872-6356
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The normal expression of ß-globin protein in mature erythrocytes is critically dependent on post-transcriptional events in erythroid progenitors that ensure the high stability of ß-globin mRNA. Previous work has revealed that these regulatory processes require AUF-1 and YB-1, two RNA-binding proteins that assemble an mRNP ß-complex on the ß-globin 3'UTR. Here, we demonstrate that the ß-complex organizes during the erythropoietic interval when both ß-globin mRNA and protein accumulate rapidly, implicating the importance of this regulatory mRNP to normal erythroid differentiation. Subsequent functional analyses link ß-complex assembly to the half-life of ß-globin mRNA in vivo, providing a mechanistic basis for this regulatory activity. AUF-1 and YB-1 appear to serve a redundant post-transcriptional function, as both ß-complex assembly and ß-globin mRNA levels are reduced by coordinate depletion of the two factors, and can be restored by independent rescue with either factor alone. Additional studies demonstrate that the ß-complex assembles more efficiently on polyadenylated transcripts, implicating a model in which the ß-complex enhances the binding of PABPC1 to the poly(A) tail, inhibiting mRNA deadenylation and consequently effecting the high half-life of ß-globin transcripts in erythroid progenitors. These data specify a post-transcriptional mechanism through which AUF1 and YB1 contribute to the normal development of erythropoietic cells, as well as to non-hematopoietic tissues in which AUF1- and YB1-based regulatory mRNPs have been observed to assemble on heterologous mRNAs.
[Mh] Termos MeSH primário: Células Eritroides/metabolismo
Ribonucleoproteínas Nucleares Heterogêneas Grupo D/metabolismo
Proteína II de Ligação a Poli(A)/metabolismo
Proteína 1 de Ligação a Y-Box/metabolismo
Globinas beta/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Diferenciação Celular
Linhagem Celular
Seres Humanos
Processamento Pós-Transcricional do RNA
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Globinas beta/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 (3' Untranslated Regions); 0 (Heterogeneous-Nuclear Ribonucleoprotein D); 0 (Poly(A)-Binding Protein II); 0 (RNA, Messenger); 0 (Y-Box-Binding Protein 1); 0 (YBX1 protein, human); 0 (beta-Globins); 0 (hnRNP D0)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150228
[St] Status:MEDLINE


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[PMID]:23966870
[Au] Autor:Goebels C; Thonn A; Gonzalez-Hilarion S; Rolland O; Moyrand F; Beilharz TH; Janbon G
[Ad] Endereço:Institut Pasteur, Unité des Aspergillus, Département Parasitologie et Mycologie, Paris, France.
[Ti] Título:Introns regulate gene expression in Cryptococcus neoformans in a Pab2p dependent pathway.
[So] Source:PLoS Genet;9(8):e1003686, 2013.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Most Cryptococccus neoformans genes are interrupted by introns, and alternative splicing occurs very often. In this study, we examined the influence of introns on C. neoformans gene expression. For most tested genes, elimination of introns greatly reduces mRNA accumulation. Strikingly, the number and the position of introns modulate the gene expression level in a cumulative manner. A screen for mutant strains able to express functionally an intronless allele revealed that the nuclear poly(A) binding protein Pab2 modulates intron-dependent regulation of gene expression in C. neoformans. PAB2 deletion partially restored accumulation of intronless mRNA. In addition, our results demonstrated that the essential nucleases Rrp44p and Xrn2p are implicated in the degradation of mRNA transcribed from an intronless allele in C. neoformans. Double mutant constructions and over-expression experiments suggested that Pab2p and Xrn2p could act in the same pathway whereas Rrp44p appears to act independently. Finally, deletion of the RRP6 or the CID14 gene, encoding the nuclear exosome nuclease and the TRAMP complex associated poly(A) polymerase, respectively, has no effect on intronless allele expression.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica
Íntrons/genética
Proteína II de Ligação a Poli(A)/genética
Estabilidade de RNA/genética
[Mh] Termos MeSH secundário: Núcleo Celular/genética
Núcleo Celular/metabolismo
Cryptococcus neoformans/genética
Redes e Vias Metabólicas/genética
Poli A/genética
Processamento de RNA/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Poly(A)-Binding Protein II); 0 (RNA, Messenger); 24937-83-5 (Poly A)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130823
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1003686


  4 / 95 MEDLINE  
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[PMID]:23440760
[Au] Autor:Fernández-Díaz Á; Bailez-Fidalgo C; Álvarez-Gutiérrez J; Buelta-González C
[Ad] Endereço:Servicio de Neurología, Hospital del Bierzo, 24411 Ponferrada, Espana. angel.puerta@telefonica.net
[Ti] Título:[A new case of oculopharyngeal dystrophy caused by pathological expansion in the PABNP1 gene].
[Ti] Título:Nuevo caso de distrofia oculofaringea por expansion patologica en el gen PABNP1..
[So] Source:Rev Neurol;56(5):302-3, 2013 Mar 01.
[Is] ISSN:1576-6578
[Cp] País de publicação:Spain
[La] Idioma:spa
[Mh] Termos MeSH primário: Distrofia Muscular Oculofaríngea/genética
Proteína II de Ligação a Poli(A)/genética
[Mh] Termos MeSH secundário: Idoso
Feminino
Seres Humanos
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Poly(A)-Binding Protein II)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:130226
[Lr] Data última revisão:
130226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130227
[St] Status:MEDLINE


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[PMID]:23382864
[Au] Autor:Kramer S; Bannerman-Chukualim B; Ellis L; Boulden EA; Kelly S; Field MC; Carrington M
[Ad] Endereço:Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
[Ti] Título:Differential localization of the two T. brucei poly(A) binding proteins to the nucleus and RNP granules suggests binding to distinct mRNA pools.
[So] Source:PLoS One;8(1):e54004, 2013.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The number of paralogs of proteins involved in translation initiation is larger in trypanosomes than in yeasts or many metazoan and includes two poly(A) binding proteins, PABP1 and PABP2, and four eIF4E variants. In many cases, the paralogs are individually essential and are thus unlikely to have redundant functions although, as yet, distinct functions of different isoforms have not been determined. Here, trypanosome PABP1 and PABP2 have been further characterised. PABP1 and PABP2 diverged subsequent to the differentiation of the Kinetoplastae lineage, supporting the existence of specific aspects of translation initiation regulation. PABP1 and PABP2 exhibit major differences in intracellular localization and distribution on polysome fractionation under various conditions that interfere with mRNA metabolism. Most striking are differences in localization to the four known types of inducible RNP granules. Moreover, only PABP2 but not PABP1 can accumulate in the nucleus. Taken together, these observations indicate that PABP1 and PABP2 likely associate with distinct populations of mRNAs. The differences in localization to inducible RNP granules also apply to paralogs of components of the eIF4F complex: eIF4E1 showed similar localization pattern to PABP2, whereas the localisation of eIF4E4 and eIF4G3 resembled that of PABP1. The grouping of translation initiation as either colocalizing with PABP1 or with PABP2 can be used to complement interaction studies to further define the translation initiation complexes in kinetoplastids.
[Mh] Termos MeSH primário: Fator de Iniciação 4E em Eucariotos/metabolismo
Evolução Molecular
Proteína I de Ligação a Poli(A)/metabolismo
Trypanosoma brucei brucei/genética
[Mh] Termos MeSH secundário: Núcleo Celular/ultraestrutura
Citoplasma/ultraestrutura
Seres Humanos
Filogenia
Proteína I de Ligação a Poli(A)/genética
Proteína II de Ligação a Poli(A)/genética
Proteína II de Ligação a Poli(A)/metabolismo
Ligação Proteica
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ribonucleoproteínas/genética
Trypanosoma brucei brucei/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Eukaryotic Initiation Factor-4E); 0 (Poly(A)-Binding Protein I); 0 (Poly(A)-Binding Protein II); 0 (RNA, Messenger); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130206
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0054004


  6 / 95 MEDLINE  
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[PMID]:23279110
[Au] Autor:Mallet PL; Bachand F
[Ad] Endereço:RNA Group, Department of Biochemistry, Université de Sherbrooke, Sherbrooke, QC, Canada.
[Ti] Título:A proline-tyrosine nuclear localization signal (PY-NLS) is required for the nuclear import of fission yeast PAB2, but not of human PABPN1.
[So] Source:Traffic;14(3):282-94, 2013 Mar.
[Is] ISSN:1600-0854
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nuclear poly(A)-binding proteins (PABPs) are evolutionarily conserved proteins that play key roles in eukaryotic gene expression. In the fission yeast Schizosaccharomyces pombe, the major nuclear PABP, Pab2, functions in the maturation of small nucleolar RNAs as well as in nuclear RNA decay. Despite knowledge about its nuclear functions, nothing is known about how Pab2 is imported into the nucleus. Here, we show that Pab2 contains a proline-tyrosine nuclear localization signal (PY-NLS) that is necessary and sufficient for its nuclear localization and function. Consistent with the role of karyopherin ß2 (Kapß2)-type receptors in the import of PY-NLS cargoes, we show that the fission yeast ortholog of human Kapß2, Kap104, binds to recombinant Pab2 and is required for Pab2 nuclear localization. The absence of arginine methylation in a basic region N-terminal to the PY-core motif of Pab2 did not affect its nuclear localization. However, in the context of a sub-optimal PY-NLS, we found that Pab2 was more efficiently targeted to the nucleus in the absence of arginine methylation, suggesting that this modification can affect the import kinetics of a PY-NLS cargo. Although a sequence resembling a PY-NLS motif can be found in the human Pab2 ortholog, PABPN1, our results indicate that neither a functional PY-NLS nor Kapß2 activity are required to promote entry of PABPN1 into the nucleus of human cells. Our findings describe the mechanism by which Pab2 is imported into the nucleus, providing the first example of a PY-NLS import system in fission yeast. In addition, this study suggests the existence of alternative or redundant nuclear import pathways for human PABPN1.
[Mh] Termos MeSH primário: Núcleo Celular/metabolismo
Proteína II de Ligação a Poli(A)/metabolismo
Proteína I de Ligação a Poli(A)/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
Proteínas de Schizosaccharomyces pombe/metabolismo
Schizosaccharomyces/metabolismo
beta Carioferinas/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular
Motivos de Aminoácidos
Arginina/metabolismo
Sítios de Ligação
Células HeLa
Seres Humanos
Sinais de Localização Nuclear
Proteína I de Ligação a Poli(A)/química
Proteína I de Ligação a Poli(A)/genética
Proteína II de Ligação a Poli(A)/química
Proteína II de Ligação a Poli(A)/genética
Proteínas de Ligação a Poli(A)/genética
Prolina/química
Transporte Proteico
Schizosaccharomyces/genética
Proteínas de Schizosaccharomyces pombe/química
Proteínas de Schizosaccharomyces pombe/genética
Tirosina/química
beta Carioferinas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Kap104 protein, S pombe); 0 (Nuclear Localization Signals); 0 (PABPN1 protein, human); 0 (Pab2 protein, S pombe); 0 (Poly(A)-Binding Protein I); 0 (Poly(A)-Binding Protein II); 0 (Poly(A)-Binding Proteins); 0 (Schizosaccharomyces pombe Proteins); 0 (beta Karyopherins); 42HK56048U (Tyrosine); 94ZLA3W45F (Arginine); 9DLQ4CIU6V (Proline)
[Em] Mês de entrada:1307
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130103
[St] Status:MEDLINE
[do] DOI:10.1111/tra.12036


  7 / 95 MEDLINE  
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[PMID]:22965128
[Au] Autor:Larochelle M; Lemay JF; Bachand F
[Ad] Endereço:Department of Biochemistry, RNA Group, Université de Sherbrooke, Sherbrooke, Quebec, Canada J1H 5N4.
[Ti] Título:The THO complex cooperates with the nuclear RNA surveillance machinery to control small nucleolar RNA expression.
[So] Source:Nucleic Acids Res;40(20):10240-53, 2012 Nov 01.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:THO is a multi-protein complex that promotes coupling between transcription and mRNA processing. In contrast to its role in mRNA biogenesis, we show here that the fission yeast THO complex negatively controls the expression of non-coding small nucleolar (sno) RNAs. Accordingly, the deletion of genes encoding subunits of the evolutionarily conserved THO complex results in increased levels of mature snoRNAs. We also show physical and functional connections between THO and components of the TRAMP polyadenylation complex, whose loss of function also results in snoRNA accumulation. Consistent with a role in snoRNA expression, we demonstrate that THO and TRAMP complexes are recruited to snoRNA genes, and that a functional THO complex is required to maintain TRAMP occupancy at sites of snoRNA transcription. Our findings suggest that THO promotes exosome-mediated degradation of snoRNA precursors by ensuring the presence of the TRAMP complex at snoRNA genes. This study unveils an unexpected role for THO in the control of snoRNA expression and provides a new link between transcription and nuclear RNA decay.
[Mh] Termos MeSH primário: Regulação Fúngica da Expressão Gênica
Proteínas Nucleares/metabolismo
Estabilidade de RNA
RNA Nucleolar Pequeno/genética
Proteínas de Schizosaccharomyces pombe/metabolismo
[Mh] Termos MeSH secundário: Núcleo Celular/enzimologia
Núcleo Celular/genética
Complexo Multienzimático de Ribonucleases do Exossomo/metabolismo
Deleção de Genes
Proteínas Nucleares/genética
Proteína II de Ligação a Poli(A)/metabolismo
Poliadenilação
Polinucleotídeo Adenililtransferase/metabolismo
Processamento Pós-Transcricional do RNA
RNA Nucleolar Pequeno/metabolismo
Schizosaccharomyces/genética
Schizosaccharomyces/metabolismo
Proteínas de Schizosaccharomyces pombe/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Poly(A)-Binding Protein II); 0 (RNA, Small Nucleolar); 0 (Schizosaccharomyces pombe Proteins); EC 2.7.7.19 (Cid14 protein, S pombe); EC 2.7.7.19 (Polynucleotide Adenylyltransferase); EC 3.1.- (Exosome Multienzyme Ribonuclease Complex)
[Em] Mês de entrada:1301
[Cu] Atualização por classe:150223
[Lr] Data última revisão:
150223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120912
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gks838


  8 / 95 MEDLINE  
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[PMID]:22844456
[Au] Autor:Su YL; Wang SC; Chiang PY; Lin NY; Shen YF; Chang GD; Chang CJ
[Ad] Endereço:Graduate Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei, Taiwan.
[Ti] Título:Tristetraprolin inhibits poly(A)-tail synthesis in nuclear mRNA that contains AU-rich elements by interacting with poly(A)-binding protein nuclear 1.
[So] Source:PLoS One;7(7):e41313, 2012.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Tristetraprolin binds mRNA AU-rich elements and thereby facilitates the destabilization of mature mRNA in the cytosol. METHODOLOGY/PRINCIPAL FINDINGS: To understand how tristetraprolin mechanistically functions, we biopanned with a phage-display library for proteins that interact with tristetraprolin and retrieved, among others, a fragment of poly(A)-binding protein nuclear 1, which assists in the 3'-polyadenylation of mRNA by binding to immature poly(A) tails and thereby increases the activity of poly(A) polymerase, which is directly responsible for polyadenylation. The tristetraprolin/poly(A)-binding protein nuclear 1 interaction was characterized using tristetraprolin and poly(A)-binding protein nuclear 1 deletion mutants in pull-down and co-immunoprecipitation assays. Tristetraprolin interacted with the carboxyl-terminal region of poly(A)-binding protein nuclear 1 via its tandem zinc finger domain and another region. Although tristetraprolin and poly(A)-binding protein nuclear 1 are located in both the cytoplasm and the nucleus, they interacted in vivo in only the nucleus. In vitro, tristetraprolin bound both poly(A)-binding protein nuclear 1 and poly(A) polymerase and thereby inhibited polyadenylation of AU-rich element-containing mRNAs encoding tumor necrosis factor α, GM-CSF, and interleukin-10. A tandem zinc finger domain-deleted tristetraprolin mutant was a less effective inhibitor. Expression of a tristetraprolin mutant restricted to the nucleus resulted in downregulation of an AU-rich element-containing tumor necrosis factor α/luciferase mRNA construct. CONCLUSION/SIGNIFICANCE: In addition to its known cytosolic mRNA-degrading function, tristetraprolin inhibits poly(A) tail synthesis by interacting with poly(A)-binding protein nuclear 1 in the nucleus to regulate expression of AU-rich element-containing mRNA.
[Mh] Termos MeSH primário: Elementos Ricos em Adenilato e Uridilato
Núcleo Celular/metabolismo
Poli A/biossíntese
Proteína II de Ligação a Poli(A)/metabolismo
Tristetraprolina/metabolismo
[Mh] Termos MeSH secundário: Animais
Células HEK293
Seres Humanos
Luciferases/genética
Camundongos
Proteína II de Ligação a Poli(A)/química
Poliadenilação
Polinucleotídeo Adenililtransferase/antagonistas & inibidores
Polinucleotídeo Adenililtransferase/metabolismo
Ligação Proteica
Estrutura Terciária de Proteína
RNA Mensageiro/biossíntese
RNA Mensageiro/química
RNA Mensageiro/genética
Tristetraprolina/química
Fator de Necrose Tumoral alfa/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Poly(A)-Binding Protein II); 0 (RNA, Messenger); 0 (Tristetraprolin); 0 (Tumor Necrosis Factor-alpha); 24937-83-5 (Poly A); EC 1.13.12.- (Luciferases); EC 2.7.7.19 (Polynucleotide Adenylyltransferase)
[Em] Mês de entrada:1211
[Cu] Atualização por classe:150224
[Lr] Data última revisão:
150224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120731
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0041313


  9 / 95 MEDLINE  
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[PMID]:22817818
[Au] Autor:Chien YY
[Ad] Endereço:Department of Neurology Keelung Chang Gung Memorial Hospital, Keelung, Taiwan. yyccsubo@adm.cgmh.org.tw
[Ti] Título:Oculopharyngeal muscular dystrophy --an under-diagnosed disease in China? Report a China-born Chinese with PABPN1 mutation and epidemiology review of the literature.
[So] Source:J Formos Med Assoc;111(7):397-402, 2012 Jul.
[Is] ISSN:0929-6646
[Cp] País de publicação:Singapore
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/PURPOSE: Most reports about oculopharyngeal muscular dystrophy (OPMD) have been contributed by occidental countries, and most of the victims of this disease are racially white. In contrast, this disorder is rarely seen in Asians and has only one African report. Consequently, OPMD has been regarded as a disease of the Western world. The purpose of this paper is to challenge the accuracy of this concept. METHODS: In a Chinese immigrant family, 3 patients manifesting signs related to OPMD were examined. Electromyography, nerve conduction studies, muscle biopsy and genetic analysis were performed on the proband. All the 322 papers about OPMD were reviewed and their country of origin was labeled to perceive the approximate prevalence of OPMD. Countries were categorized into groups according to the continents to which they belonged. RESULTS: The proband's muscle histopathology showed small angulated fiber with rimmed vacuoles, ultrastructural pathology exposed filamentous intranuclear inclusions, and genetic analysis of the polyadenylate binding protein nuclear 1(PABPN1) gene revealed 13 GCG trinucleotide repeats in one allele (GCG)13 while being normal in the other. The survey of the country of origin of OPMD reports showed that 80% of these papers were contributed by occidental countries and that the number of publications of OPMD among countries of Americas and Asia were unequal, when compared to those of European countries, which were fairly proportioned. An epidemiologic review of the literature is presented and the prevalence of OPMD is discussed. CONCLUSION: This is a China-born Chinese patient with both morphologically and genetically proven of OPMD. The very low OPMD report rate in developing countries of East Asia is due to the unfamiliarity of medical workers to OPMD and the unavailability of medical supplies to confirm the diagnosis. In addition, the present and previous reports provide clear evidence that OPMD in these areas is underdiagnosed.
[Mh] Termos MeSH primário: Distrofia Muscular Oculofaríngea/epidemiologia
Proteína II de Ligação a Poli(A)/genética
Proteína I de Ligação a Poli(A)/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Américas/epidemiologia
Ásia/epidemiologia
China/epidemiologia
Eletromiografia
Europa (Continente)/epidemiologia
Feminino
Técnicas de Genotipagem
Seres Humanos
Masculino
Meia-Idade
Distrofia Muscular Oculofaríngea/diagnóstico
Distrofia Muscular Oculofaríngea/genética
Condução Nervosa/fisiologia
Prevalência
Repetições de Trinucleotídeos/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (PABPN1 protein, human); 0 (Poly(A)-Binding Protein I); 0 (Poly(A)-Binding Protein II)
[Em] Mês de entrada:1212
[Cu] Atualização por classe:161013
[Lr] Data última revisão:
161013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120724
[St] Status:MEDLINE
[do] DOI:10.1016/j.jfma.2011.06.017


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[PMID]:22697391
[Au] Autor:Kölbel K; Ihling C; Kühn U; Neundorf I; Otto S; Stichel J; Robaa D; Beck-Sickinger AG; Sinz A; Wahle E
[Ad] Endereço:Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, Germany.
[Ti] Título:Peptide backbone conformation affects the substrate preference of protein arginine methyltransferase I.
[So] Source:Biochemistry;51(27):5463-75, 2012 Jul 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Asymmetric dimethylation of arginine side chains is a common post-translational modification of eukaryotic proteins, which serves mostly to regulate protein-protein interactions. The modification is catalyzed by type I protein arginine methyltransferases, PRMT1 being the predominant member of the family. Determinants of substrate specificity of these enzymes are poorly understood. The Nuclear poly(A) binding protein 1 (PABPN1) is methylated by PRMT1 at 13 arginine residues located in RXR sequences in the protein's C-terminal domain. We have identified a preferred site for PRMT1-catalyzed methylation in PABPN1 and in a corresponding synthetic peptide. Variants of these substrates were analyzed by steady-state kinetic analysis and mass spectrometry. The data indicate that initial methylation is directed toward the preferred arginine residue by an N-terminally adjacent proline. Enhanced methylation upon peptide cyclization suggests that induction of a reverse turn structure is the basis for the ability of the respective proline residue to enable preferred methylation of the neighboring arginine residue, and this notion is supported by far-UV circular dichroism spectroscopy. We suggest that the formation of a reverse turn facilitates the access of arginine side chains to the active sites of PRMT1, which are located in the central cavity of a doughnut-shaped PRMT1 homodimer.
[Mh] Termos MeSH primário: Peptídeos/química
Proteína-Arginina N-Metiltransferases/química
Proteína-Arginina N-Metiltransferases/metabolismo
Proteínas Repressoras/química
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência de Aminoácidos
Animais
Biocatálise
Seres Humanos
Metilação
Modelos Moleculares
Dados de Sequência Molecular
Mutagênese Sítio-Dirigida
Mutação
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/metabolismo
Proteína II de Ligação a Poli(A)/química
Proteína II de Ligação a Poli(A)/genética
Prolina
Ratos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Peptide Fragments); 0 (Peptides); 0 (Poly(A)-Binding Protein II); 0 (Repressor Proteins); 9DLQ4CIU6V (Proline); EC 2.1.1.319 (PRMT1 protein, human); EC 2.1.1.319 (PRMT1 protein, rat); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases)
[Em] Mês de entrada:1212
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120616
[St] Status:MEDLINE



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