Search results for "DNA ligase"

showing 9 items of 19 documents

Oxidative DNA base damage induced by singlet oxygen and photosensitization: recognition by repair endonucleases and mutagenicity.

2000

We have analyzed the recognition by various repair endonucleases of DNA base modifications induced by three oxidants, viz. [4-(tert-butyldioxycarbonyl)benzyl]triethylammonium chloride (BCBT), a photochemical source of tert-butoxyl radicals, disodium salt of 1,4-etheno-2,3-benzodioxin-1,4-dipropanoic acid (NDPO(2)), a chemical source of singlet oxygen, and riboflavin, a type-I photosensitizer. The base modifications induced by BCBT, which were previously shown to be mostly 7,8-dihydro-8-oxoguanine (8-oxoGua) residues, were recognized by Fpg and Ogg1 proteins, but not by endonuclease IIII, Ntg1 and Ntg2 proteins. In the case of singlet oxygen induced damage, 8-oxoGua accounted for only 35% of…

GuanineDNA LigasesLightGuanineDNA damageRiboflavinMolecular Sequence DataToxicologySubstrate Specificitychemistry.chemical_compoundEndonucleaseBacterial ProteinsGeneticsPhotosensitizerPentosyltransferasesMolecular BiologybiologyBase SequenceSinglet oxygenEscherichia coli ProteinsMutagenesisCorticoviridaeProteinsEndonucleasesDNA-(apurinic or apyrimidinic site) lyaseOxygenBiochemistrychemistryDNA ViralMutationbiology.proteinOxidation-ReductionDNADNA DamageMutation research
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The elemental role of iron in DNA synthesis and repair

2017

Iron is an essential redox element that functions as a cofactor in many metabolic pathways. Critical enzymes in DNA metabolism, including multiple DNA repair enzymes (helicases, nucleases, glycosylases, demethylases) and ribonucleotide reductase, use iron as an indispensable cofactor to function. Recent striking results have revealed that the catalytic subunit of DNA polymerases also contains conserved cysteine-rich motifs that bind iron–sulfur (Fe/S) clusters that are essential for the formation of stable and active complexes. In line with this, mitochondrial and cytoplasmic defects in Fe/S cluster biogenesis and insertion into the nuclear iron-requiring enzymes involved in DNA synthesis a…

Iron-Sulfur Proteins0301 basic medicineDNA RepairDNA polymeraseDNA damageDNA repairIronBiophysicsDNA repairEukaryotic DNA replicationSaccharomyces cerevisiaeBiochemistryDNA GlycosylasesBiomaterials03 medical and health sciencesRibonucleotide ReductasesHumansProtein–DNA interactionRibonucleotide reductaseReplication protein Achemistry.chemical_classificationDNA ligaseDeoxyribonucleasesDNA synthesis030102 biochemistry & molecular biologybiologyIron deficiencyDNA HelicasesMetals and AlloysHelicaseDNAYeast030104 developmental biologyIron cofactorBiochemistrychemistryChemistry (miscellaneous)biology.proteinIron-sulfur clusterMetallomics
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Novel isatin-derived molecules activate p53 via interference with Mdm2 to promote apoptosis

2018

International audience; The p53 protein is a key tumor suppressor in mammals. In response to various forms of genotoxic stress p53 stimulates expression of genes whose products induce cell cycle arrest and/or apoptosis. An E3-ubiquitin ligase, Mdm2 (mouse-double-minute 2) and its human ortholog Hdm2, physically interact with the amino-terminus of p53 to mediate its ubiquitin-mediated degradation via the proteasome. Thus, pharmacological inhibition of the p53-Mdm2 interaction leads to overall stabilization of p53 and stimulation of its anti-tumorigenic activity. In this study we characterize the biological effects of a novel class of non-genotoxic isatin Schiff and Mannich base derivatives (…

Isatin0301 basic medicineProgrammed cell deathCell cycle checkpointAntineoplastic AgentsApoptosis[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyPiperazinesHistonesMice03 medical and health scienceschemistry.chemical_compound0302 clinical medicineNutlinCell Line TumorProto-Oncogene ProteinsAnimalsHumansMolecular Biologychemistry.chemical_classificationDNA ligaseIsatinImidazolesISMBDsProto-Oncogene Proteins c-mdm2Cell BiologyNutlinp53-activating moleculesCell biology030104 developmental biologychemistryProteasomeApoptosis030220 oncology & carcinogenesisbiology.proteinMdm2PumaTumor Suppressor Protein p53Apoptosis Regulatory Proteinsautomated microscopy system OperettaResearch PaperDevelopmental BiologyCell Cycle
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Age-dependent changes in the transcription profile of long-lived Drosophila over-expressing glutamate cysteine ligase

2011

Abstract In our prior studies ( Orr et al., 2005 ) we achieved a 30–50% increase in the life span of Drosophila by manipulating glutathione (GSH) production in neuronal tissues, through over-expression of glutamate-cysteine ligase (GCL), a key enzyme in glutathione biosynthesis. In the present study, we identified gene response patterns from which plausible mechanisms responsible for the observed effects on life span might be inferred. Functional clustering analysis of the transcriptome data revealed that biological processes affected by GCLc in young flies (10 days) were generally related to cell morphogenesis and differentiation, while those in older flies were associated with nucleosome …

Nucleosome organizationAgingGlutamate-Cysteine LigaseLongevityBiologyTranscriptomechemistry.chemical_compoundTranscription (biology)MorphogenesisAnimalsGeneOligonucleotide Array Sequence AnalysisGeneticschemistry.chemical_classificationDNA ligaseCell morphogenesisGene Expression ProfilingfungiCell DifferentiationGlutathioneGlutathioneImmunity HumoralNucleosomesDrosophila melanogasterGCLCchemistryDevelopmental BiologyMechanisms of Ageing and Development
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Three-dimensional structure of the anaphase-promoting complex.

2001

The anaphase-promoting complex (APC) is a cell cycle-regulated ubiquitin-protein ligase, composed of at least 11 subunits, that controls progression through mitosis and G1. Using cryo-electron microscopy and angular reconstitution, we have obtained a three-dimensional model of the human APC at a resolution of 24 A. The APC has a complex asymmetric structure 140 A x 140 A x 135 A in size, in which an outer protein wall surrounds a large inner cavity. We discuss the possibility that this cavity represents a reaction chamber in which ubiquitination reactions take place, analogous to the inner cavities formed by other protein machines such as the 26S proteasome and chaperone complexes. This cag…

Protein subunitUbiquitin-Protein LigasesAnaphase-Promoting Complex-CyclosomeLigasesProtein structureUbiquitinHumansProtein Structure QuaternaryMitosisMolecular Biologychemistry.chemical_classificationDNA ligasebiologyCryoelectron MicroscopyG1 PhaseUbiquitin-Protein Ligase ComplexesCell BiologyPrecipitin TestsCell biologyProtein Structure TertiaryProteasomechemistryChaperone (protein)biology.proteinAnaphase-promoting complexHeLa CellsMolecular cell
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Novel Glutamate–Putrescine Ligase Activity in Haloferax mediterranei: A New Function for glnA-2 Gene

2021

This article belongs to the Section Cellular Biochemistry.

Salmonella typhimuriumTranscription GeneticNitrogen assimilationHaloferax mediterraneiGene ExpressionBiochemistryGlutamate-putrescine ligase activitySubstrate SpecificityLigasesAdenosine TriphosphateputrescineCloning MolecularPhylogenyhaloarchaeachemistry.chemical_classification0303 health sciencesbiologyChemistryHaloarchaeaEscherichia coli Proteinsglutamine synthetaseBioquímica y Biología MolecularQR1-502Recombinant ProteinsNitrogen assimilationHaloferax mediterraneiIsoenzymesBiochemistryArchaeal ProteinsGenetic VectorsGlutamic AcidGlutamate–putrescine ligaseMicrobiologyArticleglutamate–putrescine ligaseGlutamine synthetase03 medical and health sciencesAmmoniaGlutamine synthetaseNitrogen FixationEscherichia coliPutrescineAmino Acid SequenceMolecular Biology030304 developmental biologyDNA ligaseSequence Homology Amino Acid030306 microbiologyComputational Biologynitrogen assimilationbiology.organism_classificationMetabolic pathwayEnzymeProtein BiosynthesisHaloarchaeaGene Expression Regulation ArchaealSequence AlignmentBiomolecules
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Ubiquitin conjugating enzyme E2-N and sequestosome-1 (p62) are components of the ubiquitination process mediated by the malin-laforin E3-ubiquitin li…

2015

11 páginas, 9 figuras.

Ubiquitin-Protein LigasesUbiquitin-conjugating enzymeBiochemistryLafora diseaseSequestosome 1UbiquitinE2-conjugaseLaforinPhagosomesSequestosome-1 ProteinmedicineAutophagyLC3HumanseducationE3-ubiquitin ligaseAdaptor Proteins Signal Transducingchemistry.chemical_classificationDNA ligaseeducation.field_of_studybiologyUbiquitinationAutophagosomesCell Biologymedicine.diseaseProtein Tyrosine Phosphatases Non-ReceptorMalinUbiquitin ligaseCell biologyp62 (SQSTM1)UBE2NHEK293 CellschemistryBiochemistryGene Knockdown TechniquesUbiquitin-Conjugating Enzymesbiology.proteinCarrier ProteinsLaforinUbiquitin-Conjugating Enzyme E2 NProtein Binding
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A Solution to the Problem of the Maximal Number of Symbols for Biomolecular Computer

2019

The authors present a solution to the problem of generating the maximum possible number of symbols for a biomolecular computer using restriction enzyme BbvI and ligase as the hardware, and transition molecules built of double-stranded DNA as the software. The presented solution offers an answer to the open question, in the algorithm form, of the maximal number of symbols for a biomolecular computer that makes use of the restriction enzyme BbvI.

chemistry.chemical_classificationDNA ligaseComputer sciencebusiness.industrybiomolecular systemsbiomolecular computerComputer Science ApplicationsTheoretical Computer ScienceDNA computingRestriction enzymeSoftwarechemistryArtificial IntelligencebusinessAlgorithmSoftwareInformatica
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Sequence-specific and DNA structure-dependent interactions of Escherichia coli MutS and human p53 with DNA

2013

Many proteins involved in DNA repair systems interact with DNA that has structure altered from the typical B-form helix. Using magnetic beads to immobilize DNAs containing various types of structures, we evaluated the in vitro binding activities of two well-characterized DNA repair proteins, Escherichia coli MutS and human p53. E. coli MutS bound to double-stranded DNAs, with higher affinity for a G/T mismatch compared to a G/A mismatch and highest affinity for larger non-B-DNA structures. E. coli MutS bound best to DNA between pH 6 and 9. Experiments discriminated between modes of p53-DNA binding, and increasing ionic strength reduced p53 binding to nonspecific double-stranded DNA, but had…

chemistry.chemical_classificationDNA ligaseDNA clampHMG-boxBase pairEscherichia coli ProteinsOsmolar ConcentrationBiophysicsDNACell BiologyBiologyBiochemistryMutS DNA Mismatch-Binding ProteinDNA binding siteBiochemistrychemistryMutS-1Escherichia coliHumansNucleic Acid ConformationProtein–DNA interactionAmino Acid SequenceTumor Suppressor Protein p53Molecular BiologyReplication protein AAnalytical Biochemistry
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