Search results for "Glycosylase"

showing 10 items of 53 documents

UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles

2006

The DNA glycosylase hOGG1 initiates base excision repair (BER) of oxidised purines in cellular DNA. Using confocal microscopy and biochemical cell fractionation experiments we show that, upon UVA irradiation of human cells, hOGG1 is recruited from a soluble nucleoplasmic localisation to the nuclear matrix. More specifically, after irradiation, hOGG1 forms foci colocalising with the nuclear speckles, organelles that are interspersed between chromatin domains and that have been associated with transcription and RNA-splicing processes. The use of mutant forms of hOGG1 unable to bind the substrate showed that relocalisation of hOGG1 does not depend on the recognition of the DNA lesion by the en…

DNA RepairTranscription GeneticUltraviolet RaysDNA repairRecombinant Fusion ProteinsGreen Fluorescent ProteinsFluorescent Antibody TechniqueBiologyDNA GlycosylasesSubstrate Specificitychemistry.chemical_compoundDNA Repair ProteinDNA-(Apurinic or Apyrimidinic Site) LyaseHumansCell NucleusGuanosineBiological TransportCell BiologyBase excision repairNuclear matrixMolecular biologyChromatinCell biologychemistryDNA glycosylaseCell fractionationReactive Oxygen SpeciesDNAHeLa CellsJournal of Cell Science
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Photogenotoxicity of folic acid.

2013

Folic acid (FA), also named vitamin B9, is an essential cofactor for the synthesis of DNA bases and other biomolecules after bioactivation by dihydrofolate reductase (DHFR). FA is photoreactive and has been shown to generate DNA modifications when irradiated with UVA (360 nm) in the presence of DNA under cell-free conditions. To investigate the relevance of this reaction for cells and tissues, we irradiated three different cell lines (KB nasopharyngeal carcinoma cells, HaCaT keratinocytes, and a melanoma cell line) in the presence of FA and quantified cytotoxicity and DNA damage generation. The results indicate that FA is phototoxic and photogenotoxic by two different mechanisms. First, ext…

DNA damageCell SurvivalAntineoplastic AgentsBiochemistrychemistry.chemical_compoundFolic AcidPhysiology (medical)Cell Line TumorDihydrofolate reductaseHumansCell ProliferationbiologyDNA synthesisChemistrySuperoxide DismutaseCatalasePhotochemical ProcessesNuclear DNAHaCaTTetrahydrofolate DehydrogenaseMethotrexateBiochemistryDNA glycosylaseCell culturebiology.proteinFolic Acid AntagonistsDrug Screening Assays AntitumorDNADNA DamageFree radical biologymedicine
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PARTIAL SEQUENCING OF THE BETA-GLUCOSIDASE-ENCODING GENE FROM YEAST STRAINS ISOLATED FROM MUSTS AND WINES

2008

The aim of the present work was the identification of the gene encoding for β-glucosidase and its partial sequencing in the strainsPichia anomala AL112,Hanseniaspora uvarum Y8 andSaccharomyces cerevisiae AL41. To this aim degenerated primers, designed on the basis of aminoacid similarities of four known yeast β-glucosidases, have been used in PCR amplifications. An expected fragment of about 200 bp was amplified from all the DNAs, cloned and sequenced. Sequence homology demonstrated for the first time the presence of a β-glucosidase encoding gene inHanseniaspora uvarum andSaccharomyces cerevisiae.

GeneticsBETA-GLUCOSIDASEbiologyPichia anomalaAscomycotaGENE PARTIAL SEQUENCINGSaccharomyces cerevisiaeSICILIAN MUSTSbiology.organism_classificationHanseniasporaSettore BIO/19 - Microbiologia GeneraleApplied Microbiology and BiotechnologyYeastGENE PARTIAL SEQUENCING; BETA-GLUCOSIDASE; SICILIAN MUSTSDNA glycosylaseβ-glucosidase gene partial sequencing Hanseniaspora uvarum Pichia anomala Saccharomyces cerevisiaeGenePichia
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Deficiency of the Cockayne syndrome B (CSB) gene aggravates the genomic instability caused by endogenous oxidative DNA base damage in mice.

2007

The Cockayne syndrome B protein (CSB) has long been known to be involved in the repair of DNA modifications that block the RNA polymerase in transcribed DNA sequences (transcription-coupled repair). Recent evidence suggests that it also has a more general role in the repair of oxidative DNA base modifications such as 7,8-dihydro-8-oxo-2'-deoxyguanosine (8-oxoG). In mammalian cells, 8-oxoG is a substrate of the repair glycosylase OGG1. Mice without this enzyme accumulate 8-oxoG in the genome and have elevated spontaneous mutation rates. To elucidate the role of CSB in the prevention of mutations by oxidative DNA base damage, we have generated mice that are deficient in Csb or Ogg1 or both ge…

Genome instabilityMaleCancer ResearchDNA repairDNA damageMice Inbred StrainsMice TransgenicBiologymedicine.disease_causeCockayne syndromeGenomic InstabilityDNA GlycosylasesMiceBacterial ProteinsGeneticsmedicineLac RepressorsAnimalsPoint MutationPoly-ADP-Ribose Binding ProteinsMolecular BiologyGeneSequence DeletionGeneticsMice KnockoutMutationPoint mutationmedicine.diseaseMolecular biologyRepressor ProteinsMutagenesis InsertionalOxidative StressDNA Repair EnzymesLiverDNA glycosylaseMutationFemaleDNA DamageOncogene
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Modulation of base excision repair of 8-oxoguanine by the nucleotide sequence.

2013

8-Oxoguanine (8-oxoG) is a major product of oxidative DNA damage, which induces replication errors and interferes with transcription. By varying the position of single 8-oxoG in a functional gene and manipulating the nucleotide sequence surrounding the lesion, we found that the degree of transcriptional inhibition is independent of the distance from the transcription start or the localization within the transcribed or the non-transcribed DNA strand. However, it is strongly dependent on the sequence context and also proportional to cellular expression of 8-oxoguanine DNA glycosylase (OGG1)-demonstrating that transcriptional arrest does not take place at unrepaired 8-oxoG and proving a causal…

GuanineBase SequenceDNA RepairTranscription GeneticNucleotidesDNA-binding domainBase excision repairDNABiologyGenome Integrity Repair and ReplicationMolecular biologyDNA GlycosylasesDNA glycosylaseGenes ReporterCoding strandGeneticsDNA supercoilHumansAP siteheterocyclic compoundsNucleotide excision repairTranscription bubbleHeLa CellsNucleic acids research
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Fanconi's anaemia cells have normal steady-state levels and repair of oxidative DNA base modifications sensitive to Fpg protein

1998

Abstract Cells from Fanconi's anaemia (FA) patients are abnormally sensitive to oxygen. However, a distinct genetic defect in either the cellular defence against reactive oxygen species (ROS) or in their metabolic generation has not been identified to date. Recently, the gene for the human 8-hydroxyguanine (8-oxoG) glycosylase, which removes this oxidative base modification from the genome, has been localized on chromosome 3p25, i.e., in the same region as the FA complementation group D (FAD) gene. We therefore studied the removal of photosensitization-induced 8-oxoG residues from the DNA of FA cells, using Fpg protein, the bacterial 8-oxoG glycosylase, to quantify the lesions by alkaline e…

GuanineDNA RepairLightDNA repairBiologyToxicologymedicine.disease_causechemistry.chemical_compoundFanconi anemiaGeneticsmedicineHumansN-Glycosyl HydrolasesMolecular BiologyGeneCells CulturedPhotosensitizing AgentsDNAmedicine.diseaseMolecular biologyNuclear DNAComplementationOxidative StressFanconi AnemiaDNA-Formamidopyrimidine GlycosylaseBiochemistrychemistryDNA glycosylaseCell DivisionOxidative stressDNAMutation Research/DNA Repair
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Widespread transcriptional gene inactivation initiated by a repair intermediate of 8-oxoguanine.

2016

DNA damage can significantly modulate expression of the affected genes either by direct structural interference with transcription components or as a collateral outcome of cellular repair attempts. Thus, DNA glycosylases of the base excision repair (BER) pathway have been implicated in negative transcriptional response to several spontaneously generated DNA base modifications, including a common oxidative DNA base modification 8-oxoguanine (8-oxoG). Here, we report that single 8-oxoG situated in the non-transcribed DNA strand of a reporter gene has a pronounced negative effect on transcription, driven by promoters of various strength and with different structural properties, including viral…

GuanineDNA RepairTranscription GeneticDNAGenome Integrity Repair and ReplicationHydroxamic AcidsResponse ElementsDNA GlycosylasesDNA-(Apurinic or Apyrimidinic Site) LyaseHumansGene SilencingPromoter Regions GeneticHeLa CellsPlasmidsSequence DeletionNucleic acids research
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Generation of reporter plasmids containing defined base modifications in the DNA strand of choice

2012

Physiological effects of DNA bases other than A, G, C, and T as well as ways of removal of such bases from genomes are studied intensely. Methods for targeted insertion of modified bases into DNA, therefore, are highly demanded in the fields of DNA repair and epigenetics. This article describes efficient procedures for incorporation of modified DNA bases into a plasmid-borne enhanced green fluorescent protein (EGFP) gene. The procedure exploits excision of a stretch of 18 nt from either the transcribed or nontranscribed DNA strand with the help of the sequence-specific nicking endonucleases Nb.Bpu10I and Nt.Bpu10I. The excised single-stranded oligonucleotide is then swapped for a synthetic …

GuanineDNA clampBase pairGreen Fluorescent ProteinsOligonucleotidesBiophysicsDNACell BiologyNicking enzymeBiologyBiochemistryDNA GlycosylasesHeavy strandBiochemistryDNA glycosylaseCoding strandPrimer (molecular biology)UracilBase PairingMolecular BiologyIn vitro recombinationPlasmidsAnalytical Biochemistry
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8-Oxo-7,8-dihydroguanine in DNA does not constitute a barrier to transcription, but is converted into transcription-blocking damage by OGG1.

2011

The common DNA base modification 8-oxo-7,8-dihydroguanine (8-oxo-G) affects the efficiency and fidelity of transcription. We constructed plasmid substrates carrying single 8-oxo-G residues, specifically positioned in the transcribed or the non-transcribed DNA strands, to investigate their effects on the expression of an EGFP reporter gene and to explore the role of base excision repair in the mechanism of transcription inhibition. We report that 8-oxo-G does not directly block transcription in cells, since a single 8-oxo-G in the transcribed DNA strand did not reduce the EGFP expression levels in repair-deficient (OGG1-null) mouse embryonic fibroblast cell lines. Rather, inhibition of trans…

GuanineGeneral transcription factorDNA RepairModels GeneticTranscription GeneticResponse elementPromoterDNA-binding domainDNABiologyGenome Integrity Repair and ReplicationMolecular biologyCell LineDNA GlycosylasesMiceCoding strandGeneticsDNA supercoilAnimalsUracilTranscription bubbleNucleotide excision repairDNA DamagePlasmidsNucleic acids research
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8-Oxoguanine DNA glycosylase (Ogg1) causes a transcriptional inactivation of damaged DNA in the absence of functional Cockayne syndrome B (Csb) prote…

2008

We have analysed the effect of oxidative guanine lesions on the expression of a transfected reporter gene in mouse embryonic fibroblasts deficient in Cockayne syndrome B protein (Csb) and/or the 8-oxoguanine DNA glycosylase (Ogg1). We used a highly sensitive flow cytometry-based approach and quantitative real-time PCR to measure the changes in gene expression caused by the presence of oxidised guanine residues generated by photosensitisation in the vector DNA. In wild-type cells, small numbers (one or three) of oxidised guanines did not affect gene expression at short times after transfections, whereas progressive reduction of the transgene expression was observed at later time points. Alth…

GuanineGuanineGreen Fluorescent ProteinsGene ExpressionBiologyHost-Cell ReactivationBiochemistryCell LineDNA GlycosylasesMicechemistry.chemical_compoundGenes ReporterGene expressionAnimalsHumansGene SilencingPoly-ADP-Ribose Binding ProteinsMolecular BiologyGeneReporter genePhotosensitizing AgentsReverse Transcriptase Polymerase Chain ReactionDNA HelicasesCell BiologyBase excision repairFlow CytometryMolecular biologyDNA Repair EnzymeschemistryDNA glycosylaseDNADNA DamageDNA Repair
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