Base de dados : MEDLINE
Pesquisa : D08.811.913.696.445.650 [Categoria DeCS]
Referências encontradas : 689 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 69 ir para página                         

  1 / 689 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28456523
[Au] Autor:Chikne V; Gupta SK; Doniger T; K SR; Cohen-Chalamish S; Waldman Ben-Asher H; Kolet L; Yahia NH; Unger R; Ullu E; Kolev NG; Tschudi C; Michaeli S
[Ad] Endereço:The Mina and Everard Goodman Faculty of Life Sciences and Advanced Materials and Nanotechnology Institute, Bar-Ilan University, Ramat-Gan 5290002, Israel.
[Ti] Título:The Canonical Poly (A) Polymerase PAP1 Polyadenylates Non-Coding RNAs and Is Essential for snoRNA Biogenesis in Trypanosoma brucei.
[So] Source:J Mol Biol;429(21):3301-3318, 2017 Oct 27.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The parasite Trypanosoma brucei is the causative agent of African sleeping sickness and is known for its unique RNA processing mechanisms that are common to all the kinetoplastidea including Leishmania and Trypanosoma cruzi. Trypanosomes possess two canonical RNA poly (A) polymerases (PAPs) termed PAP1 and PAP2. PAP1 is encoded by one of the only two genes harboring cis-spliced introns in this organism, and its function is currently unknown. In trypanosomes, all mRNAs, and non-coding RNAs such as small nucleolar RNAs (snoRNAs) and long non-coding RNAs (lncRNAs), undergo trans-splicing and polyadenylation. Here, we show that the function of PAP1, which is located in the nucleus, is to polyadenylate non-coding RNAs, which undergo trans-splicing and polyadenylation. Major substrates of PAP1 are the snoRNAs and lncRNAs. Under the silencing of either PAP1 or PAP2, the level of snoRNAs is reduced. The dual polyadenylation of snoRNA intermediates is carried out by both PAP2 and PAP1 and requires the factors essential for the polyadenylation of mRNAs. The dual polyadenylation of the precursor snoRNAs by PAPs may function to recruit the machinery essential for snoRNA processing.
[Mh] Termos MeSH primário: Poli A/genética
Poliadenilação/genética
Polinucleotídeo Adenililtransferase/genética
RNA Mensageiro/genética
RNA Nucleolar Pequeno/biossíntese
RNA não Traduzido/genética
Trypanosoma brucei brucei/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Associadas a Pancreatite
Processamento de RNA
Alinhamento de Sequência
Trypanosoma brucei brucei/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pancreatitis-Associated Proteins); 0 (REG3A protein, human); 0 (RNA, Messenger); 0 (RNA, Small Nucleolar); 0 (RNA, Untranslated); 24937-83-5 (Poly A); EC 2.7.7.19 (Polynucleotide Adenylyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


  2 / 689 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28911096
[Au] Autor:Li W; Li W; Laishram RS; Hoque M; Ji Z; Tian B; Anderson RA
[Ad] Endereço:University of Wisconsin-Madison, School of Medicine and Public Health, Madison, WI 53706, USA.
[Ti] Título:Distinct regulation of alternative polyadenylation and gene expression by nuclear poly(A) polymerases.
[So] Source:Nucleic Acids Res;45(15):8930-8942, 2017 Sep 06.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Polyadenylation of nascent RNA by poly(A) polymerase (PAP) is important for 3' end maturation of almost all eukaryotic mRNAs. Most mammalian genes harbor multiple polyadenylation sites (PASs), leading to expression of alternative polyadenylation (APA) isoforms with distinct functions. How poly(A) polymerases may regulate PAS usage and hence gene expression is poorly understood. Here, we show that the nuclear canonical (PAPα and PAPγ) and non-canonical (Star-PAP) PAPs play diverse roles in PAS selection and gene expression. Deficiencies in the PAPs resulted in perturbations of gene expression, with Star-PAP impacting lowly expressed mRNAs and long-noncoding RNAs to the greatest extent. Importantly, different PASs of a gene are distinctly regulated by different PAPs, leading to widespread relative expression changes of APA isoforms. The location and surrounding sequence motifs of a PAS appear to differentiate its regulation by the PAPs. We show Star-PAP-specific PAS usage regulates the expression of the eukaryotic translation initiation factor EIF4A1, the tumor suppressor gene PTEN and the long non-coding RNA NEAT1. The Star-PAP-mediated APA of PTEN is essential for DNA damage-induced increase of PTEN protein levels. Together, our results reveal a PAS-guided and PAP-mediated paradigm for gene expression in response to cellular signaling cues.
[Mh] Termos MeSH primário: Fator de Iniciação 4A em Eucariotos/genética
Regulação da Expressão Gênica
PTEN Fosfo-Hidrolase/genética
Polinucleotídeo Adenililtransferase/genética
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Núcleo Celular/genética
Núcleo Celular/metabolismo
Fator de Iniciação 4A em Eucariotos/metabolismo
Perfilação da Expressão Gênica
Células HEK293
Seres Humanos
Isoenzimas/antagonistas & inibidores
Isoenzimas/genética
Isoenzimas/metabolismo
Cinética
PTEN Fosfo-Hidrolase/metabolismo
Poliadenilação
Polinucleotídeo Adenililtransferase/antagonistas & inibidores
Polinucleotídeo Adenililtransferase/metabolismo
RNA Longo não Codificante/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 0 (NEAT1 long non-coding RNA, human); 0 (RNA, Long Noncoding); 0 (RNA, Messenger); 0 (RNA, Small Interfering); EC 2.7.7.- (Eukaryotic Initiation Factor-4A); EC 2.7.7.19 (Polynucleotide Adenylyltransferase); EC 2.7.7.19 (Star-PAP protein, human); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (PTEN protein, human)
[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:170916
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx560


  3 / 689 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28490506
[Au] Autor:Nousch M; Minasaki R; Eckmann CR
[Ad] Endereço:Developmental Genetics, Institute of Biology, Martin Luther University Halle-Wittenberg, 06120 Halle (Saale), Germany.
[Ti] Título:Polyadenylation is the key aspect of GLD-2 function in .
[So] Source:RNA;23(8):1180-1187, 2017 Aug.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The role of many enzymes extends beyond their dedicated catalytic activity by fulfilling important cellular functions in a catalysis-independent fashion. In this aspect, little is known about 3'-end RNA-modifying enzymes that belong to the class of nucleotidyl transferases. Among these are noncanonical poly(A) polymerases, a group of evolutionarily conserved enzymes that are critical for gene expression regulation, by adding adenosines to the 3'-end of RNA targets. In this study, we investigate whether the functions of the cytoplasmic poly(A) polymerase (cytoPAP) GLD-2 in germ cells exclusively depend on its catalytic activity. To this end, we analyzed a specific missense mutation affecting a conserved amino acid in the catalytic region of GLD-2 cytoPAP. Although this mutated protein is expressed to wild-type levels and incorporated into cytoPAP complexes, we found that it cannot elongate mRNA poly(A) tails efficiently or promote GLD-2 target mRNA abundance. Furthermore, germ cell defects in animals expressing this mutant protein strongly resemble those lacking the GLD-2 protein altogether, arguing that only the polyadenylation activity of GLD-2 is essential for gametogenesis. In summary, we propose that all known molecular and biological functions of GLD-2 depend on its enzymatic activity, demonstrating that polyadenylation is the key mechanism of GLD-2 functionality. Our findings highlight the enzymatic importance of noncanonical poly(A) polymerases and emphasize the pivotal role of poly(A) tail-centered cytoplasmic mRNA regulation in germ cell biology.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Regulação da Expressão Gênica
Poli A/metabolismo
Polinucleotídeo Adenililtransferase/metabolismo
Processamento Pós-Transcricional do RNA
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Animais Geneticamente Modificados
Caenorhabditis elegans/genética
Caenorhabditis elegans/crescimento & desenvolvimento
Proteínas de Caenorhabditis elegans/genética
Mutação de Sentido Incorreto/genética
Poliadenilação
Polinucleotídeo Adenililtransferase/genética
Estabilidade de RNA
RNA Mensageiro/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (RNA, Messenger); 24937-83-5 (Poly A); EC 2.7.7.19 (GLD-2 protein, C elegans); EC 2.7.7.19 (Polynucleotide Adenylyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170512
[St] Status:MEDLINE
[do] DOI:10.1261/rna.061473.117


  4 / 689 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28426097
[Au] Autor:Maes A; Gracia C; Innocenti N; Zhang K; Aurell E; Hajnsdorf E
[Ad] Endereço:CNRS UMR8261 (previously FRE3630) associated with University Paris Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, 13 rue P. et M. Curie, 75005 Paris, France.
[Ti] Título:Landscape of RNA polyadenylation in E. coli.
[So] Source:Nucleic Acids Res;45(5):2746-2756, 2017 Mar 17.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Polyadenylation is thought to be involved in the degradation and quality control of bacterial RNAs but relatively few examples have been investigated. We used a combination of 5΄-tagRACE and RNA-seq to analyze the total RNA content from a wild-type strain and from a poly(A)polymerase deleted mutant. A total of 178 transcripts were either up- or down-regulated in the mutant when compared to the wild-type strain. Poly(A)polymerase up-regulates the expression of all genes related to the FliA regulon and several previously unknown transcripts, including numerous transporters. Notable down-regulation of genes in the expression of antigen 43 and components of the type 1 fimbriae was detected. The major consequence of the absence of poly(A)polymerase was the accumulation of numerous sRNAs, antisense transcripts, REP sequences and RNA fragments resulting from the processing of entire transcripts. A new algorithm to analyze the position and composition of post-transcriptional modifications based on the sequence of unencoded 3΄-ends, was developed to identify polyadenylated molecules. Overall our results shed new light on the broad spectrum of action of polyadenylation on gene expression and demonstrate the importance of poly(A) dependent degradation to remove structured RNA fragments.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Escherichia coli/genética
Regulação Bacteriana da Expressão Gênica
Poliadenilação
Polinucleotídeo Adenililtransferase/metabolismo
RNA Bacteriano/metabolismo
[Mh] Termos MeSH secundário: Toxinas Bacterianas/biossíntese
Escherichia coli/metabolismo
Proteínas de Escherichia coli/genética
Genoma Bacteriano
Mutação
Polinucleotídeo Adenililtransferase/genética
RNA Antissenso/metabolismo
RNA Mensageiro/metabolismo
RNA não Traduzido/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Escherichia coli Proteins); 0 (RNA, Antisense); 0 (RNA, Bacterial); 0 (RNA, Messenger); 0 (RNA, Untranslated); EC 2.7.7.19 (Polynucleotide Adenylyltransferase); EC 2.7.7.19 (pcnB protein, E coli)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170421
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw894


  5 / 689 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28231281
[Au] Autor:Mutazono M; Morita M; Tsukahara C; Chinen M; Nishioka S; Yumikake T; Dohke K; Sakamoto M; Ideue T; Nakayama JI; Ishii K; Tani T
[Ad] Endereço:Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University, Kurokami, Chuo-ku, Kumamoto, Japan.
[Ti] Título:The intron in centromeric noncoding RNA facilitates RNAi-mediated formation of heterochromatin.
[So] Source:PLoS Genet;13(2):e1006606, 2017 Feb.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In fission yeast, the formation of centromeric heterochromatin is induced through the RNA interference (RNAi)-mediated pathway. Some pre-mRNA splicing mutants (prp) exhibit defective formation of centromeric heterochromatin, suggesting that splicing factors play roles in the formation of heterochromatin, or alternatively that the defect is caused by impaired splicing of pre-mRNAs encoding RNAi factors. Herein, we demonstrate that the splicing factor spPrp16p is enriched at the centromere, and associates with Cid12p (a factor in the RNAi pathway) and the intron-containing dg ncRNA. Interestingly, removal of the dg intron, mutations of its splice sites, or replacement of the dg intron with an euchromatic intron significantly decreased H3K9 dimethylation. We also revealed that splicing of dg ncRNA is repressed in cells and its repression depends on the distance from the transcription start site to the intron. Inefficient splicing was also observed in other intron-containing centromeric ncRNAs, dh and antisense dg, and splicing of antisense dg ncRNA was repressed in the presence of the RNAi factors. Our results suggest that the introns retained in centromeric ncRNAs work as facilitators, co-operating with splicing factors assembled on the intron and serving as a platform for the recruitment of RNAi factors, in the formation of centromeric heterochromatin.
[Mh] Termos MeSH primário: Centrômero/genética
Heterocromatina/genética
Polinucleotídeo Adenililtransferase/genética
RNA não Traduzido/genética
[Mh] Termos MeSH secundário: Íntrons/genética
Metilação
Interferência de RNA
Fatores de Processamento de RNA/genética
Schizosaccharomyces/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterochromatin); 0 (RNA Splicing Factors); 0 (RNA, Untranslated); EC 2.7.7.19 (Cid13 protein, S pombe); EC 2.7.7.19 (Polynucleotide Adenylyltransferase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170224
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006606


  6 / 689 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28151486
[Au] Autor:Yu C; Gong Y; Zhou H; Wang M; Kong L; Liu J; An T; Zhu H; Li Y
[Ad] Endereço:State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming, China.
[Ti] Título:Star-PAP, a poly(A) polymerase, functions as a tumor suppressor in an orthotopic human breast cancer model.
[So] Source:Cell Death Dis;8(2):e2582, 2017 Feb 02.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Star-PAP is a noncanonical poly(A) polymerase and required for the expression of a select set of mRNAs. However, the pathological role of Star-PAP in cancer largely remains unknown. In this study, we observed decreased expression of Star-PAP in breast cancer cell lines and tissues. Ectopic Star-PAP expression inhibited proliferation as well as colony-forming ability of breast cancer cells. In breast cancer patients, high levels of Star-PAP correlated with an improved prognosis. Moreover, by regulating the expression of BIK (BCL2-interacting killer), Star-PAP induced apoptosis of breast cancer cells through the mitochondrial pathway. The growth of breast cancer xenografts in NOD/SCID mice was also inhibited by the doxycycline-induced Star-PAP overexpression. Furthermore, Star-PAP sensitized breast cancer cells to chemotherapy drugs both in vitro and in vivo. In mammary epithelial cells, Star-PAP knockdown partially transformed these cells and induced them to undergo epithelial-mesenchymal transition (EMT). These findings suggested that Star-PAP possesses tumor-suppressing activity and can be a valuable target for developing new cancer therapeutic strategies.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Neoplasias da Mama/patologia
Polinucleotídeo Adenililtransferase/metabolismo
Proteínas Supressoras de Tumor/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Apoptose/fisiologia
Proteínas Reguladoras de Apoptose/metabolismo
Neoplasias da Mama/tratamento farmacológico
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Proliferação Celular/fisiologia
Doxiciclina/farmacologia
Células Epiteliais/efeitos dos fármacos
Células Epiteliais/metabolismo
Transição Epitelial-Mesenquimal/efeitos dos fármacos
Feminino
Seres Humanos
Células MCF-7
Camundongos
Camundongos Endogâmicos NOD
Camundongos SCID
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apoptosis Regulatory Proteins); 0 (RNA, Messenger); 0 (Tumor Suppressor Proteins); EC 2.7.7.19 (Polynucleotide Adenylyltransferase); EC 2.7.7.19 (Star-PAP protein, human); N12000U13O (Doxycycline)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170203
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2016.199


  7 / 689 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28096519
[Au] Autor:Kühn U; Buschmann J; Wahle E
[Ad] Endereço:Institute of Biochemistry and Biotechnology, Martin Luther University Halle-Wittenberg, 06099 Halle, Germany.
[Ti] Título:The nuclear poly(A) binding protein of mammals, but not of fission yeast, participates in mRNA polyadenylation.
[So] Source:RNA;23(4):473-482, 2017 Apr.
[Is] ISSN:1469-9001
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The nuclear poly(A) binding protein (PABPN1) has been suggested, on the basis of biochemical evidence, to play a role in mRNA polyadenylation by strongly increasing the processivity of poly(A) polymerase. While experiments in metazoans have tended to support such a role, the results were not unequivocal, and genetic data show that the ortholog of PABPN1, Pab2, is not involved in mRNA polyadenylation. The specific model in which PABPN1 increases the rate of poly(A) tail elongation has never been examined in vivo. Here, we have used 4-thiouridine pulse-labeling to examine the lengths of newly synthesized poly(A) tails in human cells. Knockdown of PABPN1 strongly reduced the synthesis of full-length tails of ∼250 nucleotides, as predicted from biochemical data. We have also purified Pab2 and the poly(A) polymerase, Pla1, and examined their in vitro activities. Whereas PABPN1 strongly increases the activity of its cognate poly(A) polymerase in vitro, Pab2 was unable to stimulate Pla1 to any significant extent. Thus, in vitro and in vivo data are consistent in supporting a role of PABPN1 but not Pab2 in the polyadenylation of mRNA precursors.
[Mh] Termos MeSH primário: Poli A/genética
Proteína I de Ligação a Poli(A)/genética
Proteínas de Ligação a Poli(A)/genética
Polinucleotídeo Adenililtransferase/genética
Precursores de RNA/genética
Proteínas de Schizosaccharomyces pombe/genética
Schizosaccharomyces/genética
[Mh] Termos MeSH secundário: Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Regulação da Expressão Gênica
Células HEK293
Seres Humanos
Isoenzimas/genética
Isoenzimas/metabolismo
Poli A/biossíntese
Proteína I de Ligação a Poli(A)/metabolismo
Proteínas de Ligação a Poli(A)/metabolismo
Poliadenilação
Polinucleotídeo Adenililtransferase/metabolismo
Precursores de RNA/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Schizosaccharomyces/metabolismo
Proteínas de Schizosaccharomyces pombe/metabolismo
Especificidade da Espécie
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); 0 (PABPN1 protein, human); 0 (Pab2 protein, S pombe); 0 (Poly(A)-Binding Protein I); 0 (Poly(A)-Binding Proteins); 0 (RNA Precursors); 0 (RNA, Messenger); 0 (Recombinant Proteins); 0 (Schizosaccharomyces pombe Proteins); 24937-83-5 (Poly A); EC 2.7.7.19 (Polynucleotide Adenylyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.1261/rna.057026.116


  8 / 689 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28028853
[Au] Autor:Custer TC; Walter NG
[Ad] Endereço:Program in Chemical Biology, University of Michigan, Ann Arbor, Michigan, 48109.
[Ti] Título:In vitro labeling strategies for in cellulo fluorescence microscopy of single ribonucleoprotein machines.
[So] Source:Protein Sci;26(7):1363-1379, 2017 Jul.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RNA plays a fundamental, ubiquitous role as either substrate or functional component of many large cellular complexes-"molecular machines"-used to maintain and control the readout of genetic information, a functional landscape that we are only beginning to understand. The cellular mechanisms for the spatiotemporal organization of the plethora of RNAs involved in gene expression are particularly poorly understood. Intracellular single-molecule fluorescence microscopy provides a powerful emerging tool for probing the pertinent mechanistic parameters that govern cellular RNA functions, including those of protein coding messenger RNAs (mRNAs). Progress has been hampered, however, by the scarcity of efficient high-yield methods to fluorescently label RNA molecules without the need to drastically increase their molecular weight through artificial appendages that may result in altered behavior. Herein, we employ T7 RNA polymerase to body label an RNA with a cyanine dye, as well as yeast poly(A) polymerase to strategically place multiple 2'-azido-modifications for subsequent fluorophore labeling either between the body and tail or randomly throughout the tail. Using a combination of biochemical and single-molecule fluorescence microscopy approaches, we demonstrate that both yeast poly(A) polymerase labeling strategies result in fully functional mRNA, whereas protein coding is severely diminished in the case of body labeling.
[Mh] Termos MeSH primário: RNA Polimerases Dirigidas por DNA
Corantes Fluorescentes
Polinucleotídeo Adenililtransferase
RNA Mensageiro
Proteínas de Saccharomyces cerevisiae
Saccharomyces cerevisiae/enzimologia
Coloração e Rotulagem/métodos
Proteínas Virais
[Mh] Termos MeSH secundário: RNA Polimerases Dirigidas por DNA/química
RNA Polimerases Dirigidas por DNA/metabolismo
Corantes Fluorescentes/química
Corantes Fluorescentes/metabolismo
Células HeLa
Seres Humanos
Microscopia de Fluorescência
Polinucleotídeo Adenililtransferase/química
Polinucleotídeo Adenililtransferase/metabolismo
RNA Mensageiro/biossíntese
RNA Mensageiro/química
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
Proteínas Virais/química
Proteínas Virais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fluorescent Dyes); 0 (RNA, Messenger); 0 (Saccharomyces cerevisiae Proteins); 0 (Viral Proteins); EC 2.7.7.- (bacteriophage T7 RNA polymerase); EC 2.7.7.19 (Polynucleotide Adenylyltransferase); EC 2.7.7.6 (DNA-Directed RNA Polymerases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3108


  9 / 689 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27995867
[Au] Autor:Li Z; Jiang J; Yu X; Wu C; Shen D; Feng Y
[Ad] Endereço:1​School of Life Science, Beijing Institute of Technology, Beijing, PR China.
[Ti] Título:Poly(A) polymerase I participates in the indole regulatory pathway of Pantoea agglomerans YS19.
[So] Source:Microbiology;163(2):197-206, 2017 Feb.
[Is] ISSN:1465-2080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Pantoea agglomerans YS19 is a preponderant endophytic bacterium isolated from rice. It is characterized by the formation of symplasmata, a type of multicellular aggregate structure, contributing to a strong stress resistance and specific adaptation of YS19 in endophyte-host associations. Indole is an important signal molecule in intra- or interspecies relationships, regulating a variety of bacterial behaviours such as cell aggregation and stress resistance; however, the regulatory mechanism remains an ongoing area of investigation. This study selected YS19 as a model strain to construct a mutant library, utilizing the mTn5 transposon mutagenesis method, thus obtaining a positive mutant with an indole-inhibited mutation gene. Via thermal asymmetric interlaced PCR, the mutational site was identified as the gene of pcnB, which encodes the poly(A) polymerase I to catalyse the polyadenylation of RNAs. The full length of the pcnB sequence was 1332 bp, and phylogenetic analysis revealed that pcnB is extremely conserved among strains of P. agglomerans. The expression of the gene was significantly inhibited (by 36.6 % as detected via quantitative PCR) by indole (0.5 mM). Many physiological behaviours of YS19 were affected by this mutation: the cell decay rate in the post-stationary growth phase was promoted, symplasmata formation and motility were inhibited in the late stationary growth phase and the colonization ability and growth-promoting effect of YS19 on the host plant were also inhibited. This study discusses the indole regulatory pathways from the point of RNA post-transcriptional modification, thus enriching our knowledge of polyadenylation and expanding current research ideas of indole regulation.
[Mh] Termos MeSH primário: Aderência Bacteriana/fisiologia
Indóis/metabolismo
Pantoea/metabolismo
Poliadenilação/fisiologia
Polinucleotídeo Adenililtransferase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Aderência Bacteriana/genética
Pantoea/genética
Poliadenilação/genética
Polinucleotídeo Adenililtransferase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Indoles); 8724FJW4M5 (indole); EC 2.7.7.19 (Polynucleotide Adenylyltransferase)
[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:161221
[St] Status:MEDLINE
[do] DOI:10.1099/mic.0.000415


  10 / 689 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27647534
[Au] Autor:Kashiwabara SI; Tsuruta S; Okada K; Yamaoka Y; Baba T
[Ad] Endereço:Faculty of Life and Environmental Sciences, University of Tsukuba, Ibaraki 305-8572, Japan.
[Ti] Título:Adenylation by testis-specific cytoplasmic poly(A) polymerase, PAPOLB/TPAP, is essential for spermatogenesis.
[So] Source:J Reprod Dev;62(6):607-614, 2016 Dec 20.
[Is] ISSN:1348-4400
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:The testis-specific cytoplasmic poly(A) polymerase PAPOLB/TPAP is essential for spermatogenesis. Although this enzyme is responsible for poly(A) tail extension of a subset of mRNAs in round spermatids, the stability and translational efficiency of these mRNAs are unaffected by the absence of PAPOLB. To clarify the functional importance of this enzyme's adenylation activity, we produced PAPOLB-null mice expressing a polyadenylation-defective PAPOLB mutant (PAPOLB ), in which the catalytic Asp at residue 114 was mutated to Ala. Introducing PAPOLB failed to rescue PAPOLB-null phenotypes, such as reduced expression of haploid-specific mRNAs, spermiogenesis arrest, and male infertility. These results suggest that PAPOLB regulates spermatogenesis through its adenylation activity.
[Mh] Termos MeSH primário: Citoplasma/metabolismo
Polinucleotídeo Adenililtransferase/metabolismo
Espermatogênese/fisiologia
Testículo/metabolismo
[Mh] Termos MeSH secundário: Animais
Epididimo/metabolismo
Masculino
Camundongos
Camundongos Transgênicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.7.19 (Polynucleotide Adenylyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160921
[St] Status:MEDLINE
[do] DOI:10.1262/jrd.2016-116



página 1 de 69 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde