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  1 / 8783 MEDLINE  
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[PMID]:28188342
[Au] Autor:Liu J; Zhang C
[Ad] Endereço:Department of Biological Sciences, California State Polytechnic University, Pomona, CA, 91768, USA. junjunliu@cpp.edu.
[Ti] Título:The equilibrium of ubiquitination and deubiquitination at PLK1 regulates sister chromatid separation.
[So] Source:Cell Mol Life Sci;74(12):2127-2134, 2017 Jun.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:PLK1 regulates almost every aspect of mitotic events, including mitotic entry, spindle assembly, chromosome alignment, sister chromatid segregation, metaphase-anaphase transition, cytokinesis, etc. In regulating the chromosome alignment and sister chromatid segregation, PLK1 has to be localized to and removed from kinetochores at the right times, and the underlying mechanism that regulates PLK1 both spatially and temporally only became clearer recently. It has been found that deubiquitination and ubiquitination of PLK1 are responsible for its localization to and dissociation from the kinetochores, respectively. The equilibrium of this ubiquitination and deubiquitination plays an important role in regulating proper chromosome alignment and timely sister chromatid segregation. Here, we summarize and discuss the recent findings in investigating the spatial and temporal regulation of PLK1 during chromosome alignment and sister chromatid segregation.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Cromátides/metabolismo
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Proto-Oncogênicas/metabolismo
Ubiquitinação
[Mh] Termos MeSH secundário: Animais
Ciclo Celular
Humanos
Cinetocoros/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Proto-Oncogene Proteins); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (polo-like kinase 1)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2457-5


  2 / 8783 MEDLINE  
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[PMID]:28483814
[Au] Autor:Marston AL
[Ad] Endereço:The Wellcome Centre for Cell Biology, School of Biological Sciences University of Edinburgh, Edinburgh, UK.
[Ti] Título:Dalmatian: spotting the difference in cohesin protectors.
[So] Source:EMBO J;36(11):1468-1470, 2017 06 01.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The cohesin complex prevents separation of chromosomes following their duplication until the appropriate time during cell division. In vertebrates, establishment and maintenance of cohesin-dependent linkages depend on two distinct proteins, sororin and shugoshin. New findings published in show that in , the function of both of these cohesin regulators is carried out by a single hybrid protein, Dalmatian.
[Mh] Termos MeSH primário: Cromátides
Proteínas Nucleares/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Ciclo Celular/genética
Proteínas Cromossômicas não Histona/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Chromosomal Proteins, Non-Histone); 0 (Nuclear Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201797090


  3 / 8783 MEDLINE  
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[PMID]:28471230
[Au] Autor:Yuksel S; Tasdemir S; Korkmaz S
[Ti] Título:Protective effect of thymoquinone against cyclophosphamide-induced genotoxic damage in human lymphocytes.
[So] Source:Bratisl Lek Listy;118(4):208-211, 2017.
[Is] ISSN:0006-9248
[Cp] País de publicação:Slovakia
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Protective effect of thymoquinone (TQ) against the cytotoxic and genotoxic effects of cyclophosphamide (CP) was assessed in human peripheral blood lymphocyte culture. METHODS: Mitotic indices were determined as endpoints of cytotoxicity, while sister chromatid exchanges (SCE) served as endpoints of genotoxicity. Firstly, the genotoxic effect of 0.16 µg/ml of CP was tested and CP was detected as genotoxic. In the second set, CP group was treated with 20 µM and 40 µM TQ. RESULTS: TQ reduced the SCE frequencies, suggesting its protective action on human lymphocytes in vitro against the CP induced genotoxic damage. CONCLUSIONS: Our results suggest that TQ produces a protective mechanism against CP-induced genetic damage, and suggest a role of DNA strand breaks in the genotoxicity (Tab. 1, Fig. 1, Ref. 19).
[Mh] Termos MeSH primário: Benzoquinonas/farmacologia
Ciclofosfamida/toxicidade
Troca de Cromátide Irmã/efeitos de drogas
[Mh] Termos MeSH secundário: Células Cultivadas
Aberrações Cromossômicas/induzido quimicamente
Dano ao DNA/efeitos de drogas
Humanos
Linfócitos T/efeitos de drogas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoquinones); 490-91-5 (thymoquinone); 8N3DW7272P (Cyclophosphamide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.4149/BLL_2017_041


  4 / 8783 MEDLINE  
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[PMID]:28062851
[Au] Autor:Zanini IM; Soneson C; Lorenzi LE; Azzalin CM
[Ad] Endereço:Institute of Biochemistry (IBC), Department of Biology, Eidgenössische Technische Hochschule Zürich (ETHZ), Zürich CH-8093, Switzerland.
[Ti] Título:Human cactin interacts with DHX8 and SRRM2 to assure efficient pre-mRNA splicing and sister chromatid cohesion.
[So] Source:J Cell Sci;130(4):767-778, 2017 Feb 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cactins constitute a family of eukaryotic proteins broadly conserved from yeast to human and required for fundamental processes such as cell proliferation, genome stability maintenance, organismal development and immune response. Cactin proteins have been found to associate with the spliceosome in several model organisms, nevertheless their molecular functions await elucidation. Here we show that depletion of human cactin leads to premature sister chromatid separation, genome instability and cell proliferation arrest. Moreover, cactin is essential for efficient splicing of thousands of pre-mRNAs, and incomplete splicing of the pre-mRNA of sororin (also known as CDCA5), a cohesin-associated factor, is largely responsible for the aberrant chromatid separation in cactin-depleted cells. Lastly, cactin physically and functionally interacts with the spliceosome-associated factors DHX8 and SRRM2. We propose that cellular complexes comprising cactin, DHX8 and SRRM2 sustain precise chromosome segregation, genome stability and cell proliferation by allowing faithful splicing of specific pre-mRNAs. Our data point to novel pathways of gene expression regulation dependent on cactin, and provide an explanation for the pleiotropic dysfunctions deriving from cactin inactivation in distant eukaryotes.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Cromátides/metabolismo
RNA Helicases DEAD-box/metabolismo
Precursores de RNA/genética
Fatores de Processamento de RNA/metabolismo
Processamento de RNA/genética
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Ciclo Celular
Proteínas de Ciclo Celular/metabolismo
Forma do Núcleo Celular
Proliferação de Células
Instabilidade Genômica
Células HEK293
Células HeLa
Humanos
Íntrons/genética
Ligação Proteica
Precursores de RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (CDCA5 protein, human); 0 (Carrier Proteins); 0 (Cell Cycle Proteins); 0 (RNA Precursors); 0 (RNA Splicing Factors); 0 (RNA-Binding Proteins); 0 (SRRM2 protein, human); 0 (cactin protein, human); EC 3.6.4.13 (DEAD-box RNA Helicases); EC 3.6.4.13 (DHX8 protein, human)
[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:170107
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.194068


  5 / 8783 MEDLINE  
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[PMID]:28108507
[Au] Autor:Gaymes TJ; Mohamedali A; Eiliazadeh AL; Darling D; Mufti GJ
[Ad] Endereço:Department of Haematological Medicine, King's College London, Leukaemia Sciences Laboratories, The Rayne Institute, London, United Kingdom.
[Ti] Título:FLT3 and JAK2 Mutations in Acute Myeloid Leukemia Promote Interchromosomal Homologous Recombination and the Potential for Copy Neutral Loss of Heterozygosity.
[So] Source:Cancer Res;77(7):1697-1708, 2017 Apr 01.
[Is] ISSN:1538-7445
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acquired copy neutral LOH (CN-LOH) is a frequent occurrence in myeloid malignancies and is often associated with resistance to standard therapeutic modalities and poor survival. Here, we show that constitutive signaling driven by mutated FLT3 and JAK2 confers interchromosomal homologous recombination (iHR), a precedent for CN-LOH. Using a targeted recombination assay, we determined significant iHR activity in internal tandem duplication FLT3 (FLT3-ITD) and JAK2V617F-mutated cells. Sister chromatid exchanges, a surrogate measure of iHR, was significantly elevated in primary FLT3-ITD normal karyotype acute myeloid leukemia (NK-AML) compared with wild-type FLT3 NK-AML. HR was harmonized to S phase of the cell cycle to repair broken chromatids and prevent iHR. Increased HR activity in G arrested primary FLT3-ITD NK-AML in contrast to wild-type FLT3 NK-AML. Cells expressing mutated FLT3-ITD demonstrated a relative increase in mutation frequency as detected by thymidine kinase (TK) gene mutation assay. Moreover, resistance was associated with CN-LOH at the TK locus. Treatment of FLT3-ITD- and JAK2V617F-mutant cells with the antioxidant -acetylcysteine diminished reactive oxygen species (ROS), restoring iHR and HR levels. Our findings show that mutated FLT3-ITD and JAK2 augment ROS production and HR, shifting the cellular milieu toward illegitimate recombination events such as iHR and CN-LOH. Therapeutic reduction of ROS may thus prevent leukemic progression and relapse in myeloid malignancies. .
[Mh] Termos MeSH primário: Recombinação Homóloga
Janus Quinase 2/genética
Leucemia Mieloide Aguda/genética
Perda de Heterozigosidade
Mutação
Tirosina Quinase 3 Semelhante a fms/genética
[Mh] Termos MeSH secundário: Acetilcisteína/farmacologia
Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Linhagem Celular Tumoral
Criança
Humanos
Leucemia Mieloide Aguda/metabolismo
Meia-Idade
Rad51 Recombinase/fisiologia
Espécies de Oxigênio Reativas/metabolismo
Troca de Cromátide Irmã
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Reactive Oxygen Species); EC 2.7.10.1 (FLT3 protein, human); EC 2.7.10.1 (fms-Like Tyrosine Kinase 3); EC 2.7.10.2 (JAK2 protein, human); EC 2.7.10.2 (Janus Kinase 2); EC 2.7.7.- (RAD51 protein, human); EC 2.7.7.- (Rad51 Recombinase); WYQ7N0BPYC (Acetylcysteine)
[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:170121
[St] Status:MEDLINE
[do] DOI:10.1158/0008-5472.CAN-16-1678


  6 / 8783 MEDLINE  
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[PMID]:27996347
[Au] Autor:Atli Sekeroglu Z; Kefelioglu H; Kontas Yedier S; Sekeroglu V; Delmecioglu B
[Ad] Endereço:a Department of Biology, Faculty of Science and Letters , Ordu University , Ordu , Turkey.
[Ti] Título:Oxcarbazepine-induced cytotoxicity and genotoxicity in human lymphocyte cultures with or without metabolic activation.
[So] Source:Toxicol Mech Methods;27(3):201-206, 2017 Mar.
[Is] ISSN:1537-6524
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:There has been considerable debate about the relationship between epilepsy and cancer. Oxcarbazepine (OXC) is used for treating certain types of seizures in patients with epilepsy. There have been no detailed investigations about genotoxicity of OXC and its metabolites. Therefore, the aim of this study is to investigate the cytotoxic and genotoxic effects of OXC and its metabolites on cultured human lymphocytes. The cytotoxicity and genotoxicity of OXC on human peripheral blood lymphocytes were examined in vitro by sister chromatid exchange (SCE), chromosomal aberration (CA) and micronucleus (MN) tests. Cultures were treated with 125, 250 and 500 µg/ml of OXC in the presence (3 h treatment) and absence (24 h and 48 h treatment) of a metabolic activator (S9 mix). Dimethyl sulfoxide (DMSO) was used as a solvent control. OXC showed cytotoxic activities due to significant decreases in mitotic index (MI), proliferation index (PI) and nuclear division index (NDI) in the absence of S9 mix when compared with solvent control. Metabolites of OXC also significantly reduced MI and PI in cultures with S9 mix. OXC significantly increased the CAs, aberrant cells, SCE and MN values in the presence and absence of S9 mix. Our results indicated that both OXC and its metabolites have cytotoxic, cytostatic and genotoxic potential on human peripheral blood lymphocyte cultures under the experimental conditions. Further studies are necessary to elucidate the relationship between cytotoxic, cytostatic and genotoxic effects, and to make a possible risk assessment in patients receiving therapy with this drug.
[Mh] Termos MeSH primário: Anticonvulsivantes/toxicidade
Carbamazepina/análogos & derivados
Aberrações Cromossômicas/induzido quimicamente
Linfócitos/efeitos de drogas
Mutagênicos/toxicidade
Troca de Cromátide Irmã/efeitos de drogas
[Mh] Termos MeSH secundário: Adulto
Anticonvulsivantes/metabolismo
Carbamazepina/metabolismo
Carbamazepina/toxicidade
Sobrevivência Celular/efeitos de drogas
Células Cultivadas
Relação Dose-Resposta a Droga
Feminino
Voluntários Saudáveis
Humanos
Linfócitos/metabolismo
Masculino
Micronúcleos com Defeito Cromossômico/induzido quimicamente
Microssomos Hepáticos/metabolismo
Mutagênicos/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticonvulsants); 0 (Mutagens); 33CM23913M (Carbamazepine); VZI5B1W380 (oxcarbazepine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161220
[St] Status:MEDLINE
[do] DOI:10.1080/15376516.2016.1273430


  7 / 8783 MEDLINE  
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[PMID]:28381587
[Au] Autor:Zhao Y; Dominska M; Petrova A; Bagshaw H; Kokoska RJ; Petes TD
[Ad] Endereço:Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, North Carolina 27710.
[Ti] Título:Properties of Mitotic and Meiotic Recombination in the Tandemly-Repeated Gene Cluster in the Yeast .
[So] Source:Genetics;206(2):785-800, 2017 Jun.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the yeast , the genes encoding the metallothionein protein Cup1 are located in a tandem array on chromosome VIII. Using a diploid strain that is heterozygous for an insertion of a selectable marker ( ) within this tandem array, and heterozygous for markers flanking the array, we measured interhomolog recombination and intra/sister chromatid exchange in the locus. The rate of intra/sister chromatid recombination exceeded the rate of interhomolog recombination by >10-fold. Loss of the Rad51 and Rad52 proteins, required for most interhomolog recombination, led to a relatively small reduction of recombination in the array. Although interhomolog mitotic recombination in the locus is elevated relative to the average genomic region, we found that interhomolog meiotic recombination in the array is reduced compared to most regions. Lastly, we showed that high levels of copper (previously shown to elevate transcription) lead to a substantial elevation in rate of both interhomolog and intra/sister chromatid recombination in the array; recombination events that delete the insertion from the array occur at a rate of >10 /division in unselected cells. This rate is almost three orders of magnitude higher than observed for mitotic recombination events involving single-copy genes. In summary, our study shows that some of the basic properties of recombination differ considerably between single-copy and tandemly-repeated genes.
[Mh] Termos MeSH primário: Recombinação Homóloga/genética
Metalotioneína/genética
Recombinação Genética
Proteínas de Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Meiose/genética
Mitose/genética
Família Multigênica/genética
Rad51 Recombinase/genética
Proteína Rad52 de Recombinação e Reparo de DNA/genética
Saccharomyces cerevisiae/genética
Troca de Cromátide Irmã
Sequências de Repetição em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CUP1-1 protein, S cerevisiae); 0 (RAD52 protein, S cerevisiae); 0 (Rad52 DNA Repair and Recombination Protein); 0 (Saccharomyces cerevisiae Proteins); 0 (URA3 protein, S cerevisiae); 9038-94-2 (Metallothionein); EC 2.7.7.- (Rad51 Recombinase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.117.201285


  8 / 8783 MEDLINE  
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[PMID]:28249986
[Au] Autor:Prugar E; Burnett C; Chen X; Hollingsworth NM
[Ad] Endereço:Department of Biochemistry and Cell Biology, Stony Brook University, New York 11794-5215.
[Ti] Título:Coordination of Double Strand Break Repair and Meiotic Progression in Yeast by a Mek1-Ndt80 Negative Feedback Loop.
[So] Source:Genetics;206(1):497-512, 2017 May.
[Is] ISSN:1943-2631
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During meiosis, homologous chromosomes are physically connected by crossovers and sister chromatid cohesion. Interhomolog crossovers are generated by the highly regulated repair of programmed double strand breaks (DSBs). The meiosis-specific kinase Mek1 is critical for this regulation. Mek1 downregulates the mitotic recombinase Rad51, indirectly promoting interhomolog strand invasion by the meiosis-specific recombinase Dmc1. Mek1 also promotes the formation of crossovers that are distributed throughout the genome by interference and is the effector kinase for a meiosis-specific checkpoint that delays entry into Meiosis I until DSBs have been repaired. The target of this checkpoint is a meiosis-specific transcription factor, Ndt80, which is necessary to express the polo-like kinase and the cyclin thereby allowing completion of recombination and meiotic progression. This work shows that Mek1 and Ndt80 negatively feedback on each other such that when DSB levels are high, Ndt80 is inactive due to high levels of Mek1 activity. As DSBs are repaired, chromosomes synapse and Mek1 activity is reduced below a threshold that allows activation of Ndt80. Ndt80 transcription of results in degradation of Red1, a meiosis-specific protein required for Mek1 activation, thereby abolishing Mek1 activity completely. Elimination of Mek1 kinase activity allows Rad51-mediated repair of any remaining DSBs. In this way, cells do not enter Meiosis I until recombination is complete and all DSBs are repaired.
[Mh] Termos MeSH primário: Reparo do DNA/genética
Proteínas de Ligação a DNA/genética
MAP Quinase Quinase 1/genética
Meiose/genética
Rad51 Recombinase/genética
Proteínas de Saccharomyces cerevisiae/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Cromátides/genética
Pareamento Cromossômico
Segregação de Cromossomos/genética
Quebras de DNA de Cadeia Dupla
Retroalimentação Fisiológica
Fosforilação
Recombinação Genética
Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (NDT80 protein, S cerevisiae); 0 (RED1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); EC 2.7.12.2 (MAP Kinase Kinase 1); EC 2.7.7.- (Rad51 Recombinase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1534/genetics.117.199703


  9 / 8783 MEDLINE  
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[PMID]:28475600
[Au] Autor:Muñoz-Galván S; García-Rubio M; Ortega P; Ruiz JF; Jimeno S; Pardo B; Gómez-González B; Aguilera A
[Ad] Endereço:Centro Andaluz de Biología Molecular y Medicina Regenerativa-CABIMER, Universidad de Sevilla-CSIC-Universidad Pablo de Olavide, Seville, Spain.
[Ti] Título:A new role for Rrm3 in repair of replication-born DNA breakage by sister chromatid recombination.
[So] Source:PLoS Genet;13(5):e1006781, 2017 May.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Replication forks stall at different DNA obstacles such as those originated by transcription. Fork stalling can lead to DNA double-strand breaks (DSBs) that will be preferentially repaired by homologous recombination when the sister chromatid is available. The Rrm3 helicase is a replisome component that promotes replication upon fork stalling, accumulates at highly transcribed regions and prevents not only transcription-induced replication fork stalling but also transcription-associated hyper-recombination. This led us to explore the possible role of Rrm3 in the repair of DSBs when originating at the passage of the replication fork. Using a mini-HO system that induces mainly single-stranded DNA breaks, we show that rrm3Δ cells are defective in DSB repair. The defect is clearly seen in sister chromatid recombination, the major repair pathway of replication-born DSBs. Our results indicate that Rrm3 recruitment to replication-born DSBs is crucial for viability, uncovering a new role for Rrm3 in the repair of broken replication forks.
[Mh] Termos MeSH primário: Quebras de DNA de Cadeia Dupla
DNA Helicases/genética
Proteínas de Saccharomyces cerevisiae/genética
Troca de Cromátide Irmã
[Mh] Termos MeSH secundário: Cromátides/genética
DNA Helicases/metabolismo
Reparo do DNA
Replicação do DNA
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (Rrm3 protein, S cerevisiae); EC 3.6.4.- (DNA Helicases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006781


  10 / 8783 MEDLINE  
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[PMID]:28263986
[Au] Autor:Akpinar M; Lesche M; Fanourgakis G; Fu J; Anasstasiadis K; Dahl A; Jessberger R
[Ad] Endereço:Institute of Physiological Chemistry, Medical Faculty Carl Gustav Carus, Technische Universität Dresden, Dresden, Germany.
[Ti] Título:TDRD6 mediates early steps of spliceosome maturation in primary spermatocytes.
[So] Source:PLoS Genet;13(3):e1006660, 2017 Mar.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tudor containing protein 6 (TDRD6) is a male germ line-specific protein essential for chromatoid body (ChB) structure, elongated spermatid development and male fertility. Here we show that in meiotic prophase I spermatocytes TDRD6 interacts with the key protein arginine methyl transferase PRMT5, which supports splicing. TDRD6 also associates with spliceosomal core protein SmB in the absence of RNA and in an arginine methylation dependent manner. In Tdrd6-/- diplotene spermatocytes PRMT5 association with SmB and arginine dimethylation of SmB are much reduced. TDRD6 deficiency impairs the assembly of spliceosomes, which feature 3.5-fold increased levels of U5 snRNPs. In the nucleus, these deficiencies in spliceosome maturation correlate with decreased numbers of SMN-positive bodies and Cajal bodies involved in nuclear snRNP maturation. Transcriptome analysis of TDRD6-deficient diplotene spermatocytes revealed high numbers of splicing defects such as aberrant usage of intron and exons as well as aberrant representation of splice junctions. Together, this study demonstrates a novel function of TDRD6 in spliceosome maturation and mRNA splicing in prophase I spermatocytes.
[Mh] Termos MeSH primário: Proteína-Arginina N-Metiltransferases/metabolismo
Ribonucleoproteína Nuclear Pequena U5/metabolismo
Ribonucleoproteínas/genética
Ribonucleoproteínas/fisiologia
Espermatócitos/metabolismo
Spliceossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Arginina/química
Cromátides/química
Corpos Enovelados/metabolismo
Metilação de DNA
Desoxiadenosinas/química
Éxons
Ácidos Graxos Insaturados/química
Íntrons
Masculino
Metilação
Camundongos
Camundongos Transgênicos
Microscopia de Fluorescência
Domínios Proteicos
Processamento de RNA
RNA Mensageiro/metabolismo
Espermatócitos/citologia
Tionucleosídeos/química
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Deoxyadenosines); 0 (Fatty Acids, Unsaturated); 0 (RNA, Messenger); 0 (Ribonucleoprotein, U5 Small Nuclear); 0 (Ribonucleoproteins); 0 (TDRD6 protein, mouse); 0 (Thionucleosides); 634Z2VK3UQ (5'-methylthioadenosine); 94ZLA3W45F (Arginine); EC 2.1.1.319 (Prmt5 protein, mouse); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases); Y031I2N1EO (leptomycin B)
[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:170306
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006660



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