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[PMID]:29320576
[Au] Autor:Srivastava P; Sarma A; Chaturvedi CM
[Ad] Endereço:Department of Zoology, Banaras Hindu University, Varanasi, Uttar Pradesh, India.
[Ti] Título:Targeting DNA repair with PNKP inhibition sensitizes radioresistant prostate cancer cells to high LET radiation.
[So] Source:PLoS One;13(1):e0190516, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:High linear energy transfer (LET) radiation or heavy ion such as carbon ion radiation is used as a method for advanced radiotherapy in the treatment of cancer. It has many advantages over the conventional photon based radiotherapy using Co-60 gamma or high energy X-rays from a Linear Accelerator. However, charged particle therapy is very costly. One way to reduce the cost as well as irradiation effects on normal cells is to reduce the dose of radiation by enhancing the radiation sensitivity through the use of a radiomodulator. PNKP (polynucleotide kinase/phosphatase) is an enzyme which plays important role in the non-homologous end joining (NHEJ) DNA repair pathway. It is expected that inhibition of PNKP activity may enhance the efficacy of the charged particle irradiation in the radioresistant prostate cancer cell line PC-3. To test this hypothesis, we investigated cellular radiosensitivity by clonogenic cell survival assay in PC-3 cells.12Carbon ion beam of62 MeVenergy (equivalent 5.16 MeV/nucleon) and with an entrance LET of 287 kev/µm was used for the present study. Apoptotic parameters such as nuclear fragmentation and caspase-3 activity were measured by DAPI staining, nuclear ladder assay and colorimetric caspase-3method. Cell cycle arrest was determined by FACS analysis. Cell death was enhanced when carbon ion irradiation is combined with PNKPi (PNKP inhibitor) to treat cells as compared to that seen for PNKPi untreated cells. A low concentration (10µM) of PNKPi effectively radiosensitized the PC-3 cells in terms of reduction of dose in achieving the same survival fraction. PC-3 cells underwent significant apoptosis and cell cycle arrest too was enhanced at G2/M phase when carbon ion irradiation was combined with PNKPi treatment. Our findings suggest that combined treatment of carbon ion irradiation and PNKP inhibition could enhance cellular radiosensitivity in a radioresistant prostate cancer cell line PC-3. The synergistic effect of PNKPi and carbon ion irradiation could be used as a promising method for carbon-ion therapy in radioresistant cells.
[Mh] Termos MeSH primário: Reparo do DNA
Polinucleotídeo 5´-Hidroxiquinase/antagonistas & inibidores
Neoplasias da Próstata/radioterapia
Tolerância a Radiação
[Mh] Termos MeSH secundário: Relação Dose-Resposta à Radiação
Seres Humanos
Masculino
Neoplasias da Próstata/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190516


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[PMID]:28922417
[Au] Autor:Sanchez A; Gadaleta MC; Limbo O; Russell P
[Ad] Endereço:Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA, United States of America.
[Ti] Título:Lingering single-strand breaks trigger Rad51-independent homology-directed repair of collapsed replication forks in the polynucleotide kinase/phosphatase mutant of fission yeast.
[So] Source:PLoS Genet;13(9):e1007013, 2017 Sep.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The DNA repair enzyme polynucleotide kinase/phosphatase (PNKP) protects genome integrity by restoring ligatable 5'-phosphate and 3'-hydroxyl termini at single-strand breaks (SSBs). In humans, PNKP mutations underlie the neurological disease known as MCSZ, but these individuals are not predisposed for cancer, implying effective alternative repair pathways in dividing cells. Homology-directed repair (HDR) of collapsed replication forks was proposed to repair SSBs in PNKP-deficient cells, but the critical HDR protein Rad51 is not required in PNKP-null (pnk1Δ) cells of Schizosaccharomyces pombe. Here, we report that pnk1Δ cells have enhanced requirements for Rad3 (ATR/Mec1) and Chk1 checkpoint kinases, and the multi-BRCT domain protein Brc1 that binds phospho-histone H2A (γH2A) at damaged replication forks. The viability of pnk1Δ cells depends on Mre11 and Ctp1 (CtIP/Sae2) double-strand break (DSB) resection proteins, Rad52 DNA strand annealing protein, Mus81-Eme1 Holliday junction resolvase, and Rqh1 (BLM/WRN/Sgs1) DNA helicase. Coupled with increased sister chromatid recombination and Rad52 repair foci in pnk1Δ cells, these findings indicate that lingering SSBs in pnk1Δ cells trigger Rad51-independent homology-directed repair of collapsed replication forks. From these data, we propose models for HDR-mediated tolerance of persistent SSBs with 3' phosphate in pnk1Δ cells.
[Mh] Termos MeSH primário: Enzimas Reparadoras do DNA/genética
Reparo do DNA/genética
Polinucleotídeo 5´-Hidroxiquinase/genética
Rad51 Recombinase/genética
[Mh] Termos MeSH secundário: Quinase do Ponto de Checagem 1/genética
Quinase do Ponto de Checagem 2/genética
Quebras de DNA de Cadeia Dupla
Quebras de DNA de Cadeia Simples
Dano ao DNA/genética
Replicação do DNA/genética
Proteínas de Ligação a DNA/genética
Endonucleases/genética
Exodesoxirribonucleases/genética
Resolvases de Junção Holliday/genética
Seres Humanos
Mutação
Reparo de DNA por Recombinação/genética
Schizosaccharomyces/genética
Proteínas de Schizosaccharomyces pombe/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Brc1 protein, S pombe); 0 (Ctp1 protein, S pombe); 0 (DNA-Binding Proteins); 0 (MUS81 protein, S pombe); 0 (Schizosaccharomyces pombe Proteins); 0 (rad52 protein, S pombe); EC 2.7.1.11 (Checkpoint Kinase 2); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase); EC 2.7.11.1 (Checkpoint Kinase 1); EC 2.7.11.1 (Chk1 protein, S pombe); EC 2.7.11.1 (rad3 protein, S pombe); EC 2.7.7.- (Rad51 Recombinase); EC 3.1.- (Eme1protein, S pombe); EC 3.1.- (Endonucleases); EC 3.1.- (Exodeoxyribonucleases); EC 3.1.- (Mre11 protein, S pombe); EC 3.1.21.- (Holliday Junction Resolvases); EC 6.5.1.- (DNA Repair Enzymes)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007013


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[PMID]:28511668
[Au] Autor:Muruganandam G; Raasakka A; Myllykoski M; Kursula I; Kursula P
[Ad] Endereço:Centre for Structural Systems Biology - Helmholtz Centre for Infection Research, German Electron Synchrotron (DESY), Hamburg, Germany.
[Ti] Título:Structural similarities and functional differences clarify evolutionary relationships between tRNA healing enzymes and the myelin enzyme CNPase.
[So] Source:BMC Biochem;18(1):7, 2017 May 16.
[Is] ISSN:1471-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Eukaryotic tRNA splicing is an essential process in the transformation of a primary tRNA transcript into a mature functional tRNA molecule. 5'-phosphate ligation involves two steps: a healing reaction catalyzed by polynucleotide kinase (PNK) in association with cyclic phosphodiesterase (CPDase), and a sealing reaction catalyzed by an RNA ligase. The enzymes that catalyze tRNA healing in yeast and higher eukaryotes are homologous to the members of the 2H phosphoesterase superfamily, in particular to the vertebrate myelin enzyme 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase). RESULTS: We employed different biophysical and biochemical methods to elucidate the overall structural and functional features of the tRNA healing enzymes yeast Trl1 PNK/CPDase and lancelet PNK/CPDase and compared them with vertebrate CNPase. The yeast and the lancelet enzymes have cyclic phosphodiesterase and polynucleotide kinase activity, while vertebrate CNPase lacks PNK activity. In addition, we also show that the healing enzymes are structurally similar to the vertebrate CNPase by applying synchrotron radiation circular dichroism spectroscopy and small-angle X-ray scattering. CONCLUSIONS: We provide a structural analysis of the tRNA healing enzyme PNK and CPDase domains together. Our results support evolution of vertebrate CNPase from tRNA healing enzymes with a loss of function at its N-terminal PNK-like domain.
[Mh] Termos MeSH primário: 2´,3´-Nucleotídeo Cíclico Fosfodiesterases/química
Evolução Molecular
[Mh] Termos MeSH secundário: 2',3'-Nucleotídeo Cíclico Fosfodiesterases/metabolismo
2',3'-Nucleotídeo Cíclico Fosfodiesterases/fisiologia
Animais
Dicroísmo Circular
Células Eucarióticas/enzimologia
Anfioxos
Camundongos
Bainha de Mielina/enzimologia
Polinucleotídeo 5'-Hidroxiquinase/química
Polinucleotídeo 5'-Hidroxiquinase/metabolismo
Processamento de RNA
RNA de Transferência/genética
Saccharomyces cerevisiae
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
9014-25-9 (RNA, Transfer); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase); EC 3.1.4.- (2',3'-Cyclic-Nucleotide Phosphodiesterases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE
[do] DOI:10.1186/s12858-017-0084-2


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[PMID]:28107744
[Au] Autor:Li X; Xu X; Song J; Xue Q; Li C; Jiang W
[Ad] Endereço:Key Laboratory for Colloid and Interface Chemistry of Education Ministry, School of Chemistry and Chemical Engineering, Shandong University, 250100 Jinan, PR China; Department of Chemistry, Liaocheng University, Liao cheng 252059, PR China.
[Ti] Título:Sensitive detection of T4 polynucleotide kinase activity based on multifunctional magnetic probes and polymerization nicking reactions mediated hyperbranched rolling circle amplification.
[So] Source:Biosens Bioelectron;91:631-636, 2017 May 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:T4 polynucleotide kinase (PNK) plays critical roles in regulating DNA phosphorylation modes during the repair of DNA lesions. The aberrant activity of T4 PNK has been proven to be associated with a variety of human pathologies. Sensitive detection of T4 PNK activity is critical to both clinical diagnosis and therapeutics. Herein, a background-eliminated fluorescence assay for sensitive detection of T4 PNK activity has been developed by multifunctional magnetic probes and polymerization nicking reactions mediated hyperbranched rolling circle amplification (HRCA). First, the streptavidin-magnetic nanobeads (MBs) were functionalized with the biotin modified hairpin probe (HP) with 3'-phosphoryl, forming multifunctional magnetic probes (HP-MBs). Then, in the presence of T4 PNK, the 3'-phosphoryl of HP-MBs was hydrolyzed to 3'-hydroxyl, thus serving as primers to initiate the polymerization extension and nicking endonuclease cleavage reaction. Next, the primers released from above "polymerization-nicking" cycles were separated out to trigger the subsequently HRCA process, producing plenty of dsDNA. Finally, the intercalating dye SYBR Green I (SG) was inserted into the dsDNA, generating enhanced fluorescence signals. In our design, the HP-MBs here serve together as the T4 PNK, DNA polymerase, and endonuclease recognition probe, and thus avoid the demands of utilizing multiple probes design. Moreover, it performed primary "polymerization-nicking" amplification and mediate secondary HRCA. In addition to, performing the separation function, the binding of HP-MBs and SG could be avoided while a low background was acquired. This method showed excellent sensitivity with a detection limit of 0.0436 mU/mL, and accomplished exceptional characterization T4 PNK activity in cell extracts, offering a powerful tool for biomedical research and clinical diagnosis.
[Mh] Termos MeSH primário: Bacteriófago T4/enzimologia
Técnicas Biossensoriais/métodos
Polinucleotídeo 5´-Hidroxiquinase/análise
Espectrometria de Fluorescência/métodos
[Mh] Termos MeSH secundário: Sondas de DNA/química
Ensaios Enzimáticos/métodos
Células HeLa
Seres Humanos
Limite de Detecção
Imãs/química
Estreptavidina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA Probes); 9013-20-1 (Streptavidin); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170531
[Lr] Data última revisão:
170531
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE


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[PMID]:27984013
[Au] Autor:Liu H; Ma C; Wang J; Chen H; Wang K
[Ad] Endereço:State Key Laboratory of Medical Genetics & School of Life Sciences, Central South University, Changsha 410013, China.
[Ti] Título:Label-free colorimetric assay for T4 polynucleotide kinase/phosphatase activity and its inhibitors based on G-quadruplex/hemin DNAzyme.
[So] Source:Anal Biochem;517:18-21, 2017 Jan 15.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Here we report a new approach for label-free colorimetric assay of T4 polynucleotide kinase/phosphatase (PNKP) activity based on G-quadruplex/hemin DNAzyme. In the presence of T4 PNKP, the DNA primer with a 3'-phosphate can be dephosphorylated into a 3'-hydroxyl and initiate a primer elongation reaction to open the hairpin probe, and leading to releasing the G-quartets. Under optimal conditions, the proposed method exhibited a considerable performance with a detection limit of 0.01 U/mL. Furthermore, the present assay can be used to study the potential T4 PNKP inhibitor screening, making it promise to be applied in the fields of drug discovery.
[Mh] Termos MeSH primário: Bacteriófago T4/enzimologia
DNA Catalítico/química
Inibidores Enzimáticos/química
Quadruplex G
Hemina/química
Polinucleotídeo 5´-Hidroxiquinase/análise
Proteínas Virais/análise
[Mh] Termos MeSH secundário: Colorimetria/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Catalytic); 0 (Enzyme Inhibitors); 0 (Viral Proteins); 743LRP9S7N (Hemin); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE


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[PMID]:27540854
[Au] Autor:Ghosh G; Sen M
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA. Electronic address: gghosh@ucsd.edu.
[Ti] Título:A New DNA Methyltransferase-Histone Deacetylase-Kinase Axis in Innate Immunity.
[So] Source:Mol Cell;63(4):544-546, 2016 Aug 18.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Regulatory roles of protein and DNA modifications in gene expression during host defense have long been appreciated. In a recent article published in Nature Immunology, Li et al. (2016) provide a unique glimpse of yet another aspect of coordinated DNA methylation and protein acetylation in host response to pathogenic stimuli. They elegantly demonstrate that DNA methylation and transcriptional activation at the HDAC9 promoter by DNMT3a, along with lysine deacetylation of TBK1 by HDAC9, are essential events during host defense.
[Mh] Termos MeSH primário: Histona Desacetilases
Protamina Quinase
[Mh] Termos MeSH secundário: Acetilação
DNA
Metilação de DNA
Histonas
Seres Humanos
Metiltransferases
Polinucleotídeo 5'-Hidroxiquinase
Regiões Promotoras Genéticas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); 9007-49-2 (DNA); EC 2.1.1.- (Methyltransferases); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase); EC 2.7.11.1 (Protamine Kinase); EC 3.5.1.98 (Histone Deacetylases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160820
[St] Status:MEDLINE


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[PMID]:27470713
[Au] Autor:de Araujo PR; Gorthi A; da Silva AE; Tonapi SS; Vo DT; Burns SC; Qiao M; Uren PJ; Yuan ZM; Bishop AJ; Penalva LO
[Ad] Endereço:Greehey Children's Cancer Research Institute, University of Texas Health Science Center, San Antonio, Texas; Department of Cellular and Structural Biology, University of Texas Health Science Center, San Antonio, Texas.
[Ti] Título:Musashi1 Impacts Radio-Resistance in Glioblastoma by Controlling DNA-Protein Kinase Catalytic Subunit.
[So] Source:Am J Pathol;186(9):2271-8, 2016 Sep.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The conserved RNA-binding protein Musashi1 (MSI1) has been characterized as a stem cell marker, controlling the balance between self-renewal and differentiation and as a key oncogenic factor in numerous solid tumors, including glioblastoma. To explore the potential use of MSI1 targeting in therapy, we studied MSI1 in the context of radiation sensitivity. Knockdown of MSI1 led to a decrease in cell survival and an increase in DNA damage compared to control in cells treated with ionizing radiation. We subsequently examined mechanisms of double-strand break repair and found that loss of MSI1 reduces the frequency of nonhomologous end-joining. This phenomenon could be attributed to the decreased expression of DNA-protein kinase catalytic subunit, which we have previously identified as a target of MSI1. Collectively, our results suggest a role for MSI1 in double-strand break repair and that its inhibition may enhance the effect of radiotherapy.
[Mh] Termos MeSH primário: Reparo do DNA/fisiologia
Glioblastoma/patologia
Proteínas do Tecido Nervoso/metabolismo
Polinucleotídeo 5´-Hidroxiquinase/metabolismo
Proteínas de Ligação a RNA/metabolismo
Tolerância a Radiação/fisiologia
[Mh] Termos MeSH secundário: Domínio Catalítico/fisiologia
Linhagem Celular Tumoral
Ensaio Cometa
Quebras de DNA de Cadeia Dupla/efeitos da radiação
DNA Catalítico
Imunofluorescência
Seres Humanos
Immunoblotting
Reação em Cadeia da Polimerase
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Catalytic); 0 (MSI1 protein, human); 0 (Nerve Tissue Proteins); 0 (RNA-Binding Proteins); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170902
[Lr] Data última revisão:
170902
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160730
[St] Status:MEDLINE


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[PMID]:27030367
[Au] Autor:Cen Y; Yang Y; Yu RQ; Chen TT; Chu X
[Ad] Endereço:State Key Laboratory of Chemo/Bio-Sensing and Chemometrics, College of Chemistry and Chemical Engineering, Hunan University, Changsha, 410082, P. R. China. chenting1104@hnu.edu.cn xiachu@hnu.edu.cn.
[Ti] Título:A cobalt oxyhydroxide nanoflake-based nanoprobe for the sensitive fluorescence detection of T4 polynucleotide kinase activity and inhibition.
[So] Source:Nanoscale;8(15):8202-9, 2016 Apr 21.
[Is] ISSN:2040-3372
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phosphorylation of nucleic acids with 5'-OH termini catalyzed by polynucleotide kinase (PNK) is an inevitable process and has been implicated in many important cellular events. Here, we found for the first time that there was a significant difference in the adsorbent ability of cobalt oxyhydroxide (CoOOH) nanoflakes between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA), which resulted in the fluorescent dye-labeled dsDNA still retaining strong fluorescence emission, while the fluorescence signal of ssDNA was significantly quenched by CoOOH nanoflakes. Based on this discovery, we developed a CoOOH nanoflake-based nanoprobe for the fluorescence sensing of T4 PNK activity and its inhibition by combining it with λ exonuclease cleavage reaction. In the presence of T4 PNK, dye-labeled dsDNA was phosphorylated and then cleaved by λ exonuclease to generate ssDNA, which could adsorb on the CoOOH nanoflakes and whose fluorescence was quenched by CoOOH nanoflakes. Due to the high quenching property of CoOOH nanoflakes as an efficient energy acceptor, a sensitive and selective sensing approach with satisfactory performance for T4 PNK sensing in a complex biological matrix has been successfully constructed and applied to the screening of inhibitors. The developed approach may potentially provide a new platform for further research, clinical diagnosis, and drug discovery of nucleotide kinase related diseases.
[Mh] Termos MeSH primário: Bacteriófago T4/enzimologia
Nanopartículas Metálicas/química
Polinucleotídeo 5´-Hidroxiquinase/análise
Proteínas Virais/análise
[Mh] Termos MeSH secundário: Cobalto/química
Transferência Ressonante de Energia de Fluorescência
Corantes Fluorescentes
Células HeLa
Seres Humanos
Óxidos/química
Polinucleotídeo 5'-Hidroxiquinase/antagonistas & inibidores
Proteínas Virais/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fluorescent Dyes); 0 (HCoO2); 0 (Oxides); 0 (Viral Proteins); 3G0H8C9362 (Cobalt); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170309
[Lr] Data última revisão:
170309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE
[do] DOI:10.1039/c6nr01427e


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[PMID]:26807522
[Au] Autor:Xu J; Gao Y; Li B; Jin Y
[Ad] Endereço:Key Laboratory of Applied Surface and Colloid Chemistry, Ministry of Education, Key Laboratory of Analytical Chemistry for Life Science of Shaanxi Province, School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi'an 710062, China.
[Ti] Título:Cyclic up-regulation fluorescence of pyrene excimer for studying polynucleotide kinase activity based on dual amplification.
[So] Source:Biosens Bioelectron;80:91-97, 2016 Jun 15.
[Is] ISSN:1873-4235
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Due to its important biological and clinical roles of polynucleotide kinase (PNK), accurate monitoring of PNK activity and inhibition is highly desirable. Herein, a homogeneous and sensitive fluorescence assay has been proposed for the detection of PNK activity by integrating target recycling signal amplification of DNA toehold strand displacement reaction (TSDR) with gamma-cyclodextrin (γ-CD) enhancement of pyrene excimer. A label-free hairpin DNA1 (H1) and two singly pyrene-labelled DNA, H2 and H3, are designed. Accompanying the occurrence of the efficient enzyme reactions, namely phosphorylation-actuated λ exonuclease reaction, a single-stranded DNA as a trigger DNA (tDNA) of TSDR can be released from H1. Then, tDNA drives circulatory interactions between H2 and H3 to continuously form H2/H3 duplex, resulting in formation of pyrene excimer and a "turn on" fluorescence signal of pyrene excimer. Furthermore, the fluorescence of pyrene excimer is further amplified by introducing gamma-cyclodextrin (γ-CD), which can regulate the space proximity of two pyrene molecules. Thus, TSDR-induced cyclic formation of pyrene excimer and γ-CD enhancement can specifically up-regulate the fluorescence of pyrene excimer for detection of PNK activity, the detection limit is 9.3 × 10(-5)UmL(-1), which is superior to those of most existing approaches. Moreover, the proposed strategy can also be successfully utilized to study inhibition efficiency of different PNK inhibitors as well. Therefore, a dual amplification approach is provided for nucleic acid phosphorylation related researches.
[Mh] Termos MeSH primário: Técnicas Biossensoriais
DNA de Cadeia Simples/química
DNA/química
Polinucleotídeo 5´-Hidroxiquinase/isolamento & purificação
[Mh] Termos MeSH secundário: Bacteriófago T4/química
Bacteriófago T4/genética
Fluorescência
Regulação da Expressão Gênica
Fosforilação
Polinucleotídeo 5'-Hidroxiquinase/biossíntese
Pirenos/química
Espectrometria de Fluorescência
gama-Ciclodextrinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Single-Stranded); 0 (Pyrenes); 0 (gamma-Cyclodextrins); 9007-49-2 (DNA); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase); KZJ0BYZ5VA (gamma-cyclodextrin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170924
[Lr] Data última revisão:
170924
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160126
[St] Status:MEDLINE


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[PMID]:26518115
[Au] Autor:Ma C; Liu H; Du J; Chen H; He H; Jin S; Wang K; Wang J
[Ad] Endereço:State Key Laboratory of Medical Genetics & School of Life Sciences, Central South University, Changsha 410013, China; State Key Laboratory of Chemo/Biosensing and Chemometrics, Hunan University, Changsha 410081, China. Electronic address: macb2012@csu.edu.cn.
[Ti] Título:Quencher-free hairpin probes for real-time detection of T4 polynucleotide kinase activity.
[So] Source:Anal Biochem;494:1-3, 2016 Feb 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Traditional methods of assaying polynucleotide kinase (PNK) activity are discontinuous, time-consuming, and laborious. Here we report a new quencher-free approach to real-time monitoring of PNK activity using a 2-aminopurine probe. When the 2-aminopurine probe was 5'-phosphorylated by PNK, it could be efficiently degraded by lambda exonuclease to release free 2-aminopurine molecules and generate a fluorescence signal. This method not only provides a universal approach to real-time monitoring of PNK activity, but also shows great potential for screening suitable inhibitor drugs for PNK.
[Mh] Termos MeSH primário: Bacteriófago T4/enzimologia
Polinucleotídeo 5´-Hidroxiquinase/análise
Espectrometria de Fluorescência
[Mh] Termos MeSH secundário: 2-Aminopurina/metabolismo
Bacteriófago lambda/enzimologia
Exonucleases/metabolismo
Fosforilação
Polinucleotídeo 5'-Hidroxiquinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
452-06-2 (2-Aminopurine); EC 2.7.1.78 (Polynucleotide 5'-Hydroxyl-Kinase); EC 3.1.- (Exonucleases)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:151228
[Lr] Data última revisão:
151228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151101
[St] Status:MEDLINE



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