Search results for "binding proteins"

showing 10 items of 911 documents

ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1).

2000

The Myc promoter-binding protein-1 (MBP-1) is a 37-38 kDa protein that binds to the c-myc P2 promoter and negatively regulates transcription of the protooncogene. MBP-1 cDNA shares 97% similarity with the cDNA encoding the glycolytic enzyme alpha-enolase and both genes have been mapped to the same region of human chromosome 1, suggesting the hypothesis that the two proteins might be encoded by the same gene. We show here data indicating that a 37 kDa protein is alternatively translated from the full-length alpha-enolase mRNA. This shorter form of alpha-enolase is able to bind the MBP-1 consensus sequence and to downregulate expression of a luciferase reporter gene under the control of the c…

CytoplasmTranscriptional repressionRecombinant Fusion ProteinsBiophysicsEnolaseCodon InitiatorDown-RegulationBiologyAlternative translationResponse ElementsTransfectionBiochemistryCell LineGene productHSPA4Proto-Oncogene Proteins c-mycStructural BiologyHSPA2GeneticsBiomarkers TumorE2F1AnimalsHumansSOCS6Genes Tumor SuppressorDNA bindingPromoter Regions GeneticMolecular BiologyYY1Tumor Suppressor ProteinsNuclear ProteinsCell BiologyDNAMolecular biologyGPS2Neoplasm ProteinsDNA-Binding ProteinsMolecular WeightRepressor ProteinsAlternative SplicingGATAD2BChromosomes Human Pair 1Phosphopyruvate HydrataseProtein BiosynthesisPeptidesProtein BindingFEBS letters
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Targeting positive regulatory domain I-binding factor 1 and X box-binding protein 1 transcription factors by multiple myeloma-reactive CTL.

2005

Abstract Growing evidence indicates that multiple myeloma (MM) and other malignancies are susceptible to CTL-based immune interventions. We studied whether transcription factors inherently involved in the terminal differentiation of mature B lymphocytes into malignant and nonmalignant plasma cells provide MM-associated CTL epitopes. HLA-A*0201 (A2.1) transgenic mice were used to identify A2.1-presented peptide Ag derived from the plasma cell-associated transcriptional regulators, positive regulatory domain I-binding factor 1 (PRDI-BF1) and X box-binding protein 1 (XBP-1). A2.1-restricted CTL specific for PRDI-BF1 and XBP-1 epitopes efficiently killed a variety of MM targets. PRDI-BF1- and X…

Cytotoxicity ImmunologicX-Box Binding Protein 1Cellular differentiationImmunologyEpitopes T-LymphocyteMice TransgenicRegulatory Factor X Transcription FactorsBiologyEpitopeMiceImmune systemCell Line TumorHLA-A2 AntigenImmunology and AllergyAnimalsHumansTranscription factorAntigen PresentationB-LymphocytesCell DeathT-cell receptorCell DifferentiationCytotoxicity Tests ImmunologicX-Box Binding Protein 1Molecular biologyPeptide FragmentsCell biologyDNA-Binding ProteinsMice Inbred C57BLRepressor ProteinsCTL*Self ToleranceNIH 3T3 CellsPositive Regulatory Domain I-Binding Factor 1Multiple MyelomaCD8T-Lymphocytes CytotoxicTranscription FactorsJournal of immunology (Baltimore, Md. : 1950)
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Sex-specific windows for high mRNA expression of DNA methyltransferases 1 and 3A and methyl-CpG-binding domain proteins 2 and 4 in human fetal gonads

2006

DNA methyltransferases (DNMTs) and 5-methyl-CpG-binding domain proteins (MBDs) are involved in the acquisition of parent-specific epigenetic modifications in human male and female germ cells. Reverse Northern blot analyses demonstrated sex-specific differences in mRNA expression for the maintenance DNMT1 and the de novo DNMT3A in developing testis and ovary. In fetal testis DNMT1 and DNMT3A expression peaked in mitotically arrested spermatogonia around 21 weeks gestation. In fetal ovary transcriptional upregulation of DNMT1 and DNMT3A occurred during a very brief period at 16 weeks gestation, when the oocytes proceeded through meiotic prophase. Fetal gonads showed several fold higher DNMT3A…

DNA (Cytosine-5-)-Methyltransferase 1MaleMethyltransferaseEmbryonic DevelopmentGestational AgeOvaryBiologyGene Expression Regulation EnzymologicChromatin remodelingDNA Methyltransferase 3AFetal DevelopmentPregnancyTestisGeneticsmedicineHumansDNA (Cytosine-5-)-MethyltransferasesRNA MessengerEpigeneticsRegulation of gene expressionFetusReverse Transcriptase Polymerase Chain Reactionurogenital systemOvaryGene Expression Regulation DevelopmentalCell BiologyReverse northern blotMolecular biologyMethyl-CpG-binding domainCell biologyDNA-Binding Proteinsmedicine.anatomical_structureembryonic structuresFemaleTranscription FactorsDevelopmental BiologyMolecular Reproduction and Development
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Deinococcus radiodurans' SRA-HNH domain containing protein Shp (Dr1533) is involved in faithful genome inheritance maintenance following DNA damage

2018

WOS:000452343100012; International audience; Background: Deinococcus radiodurans R1 (DR) survives conditions of extreme desiccation, irradiation and exposure to genotoxic chemicals, due to efficient DNA breaks repair, also through Mn2+ protection of DNA repair enzymes. Methods: Possible annotated domains of the DR1533 locus protein (Shp) were searched by bioinformatic analysis. The gene was cloned and expressed as fusion protein. Band-shift assays of Shp or the SRA and HNH domains were performed on oligonucleotides, genomic DNA from E. coif and DR. slip knock-out mutant was generated by homologous recombination with a kanamycin resistance cassette. Results: DR1533 contains an N-terminal SRA…

DNA RepairDNA cytosine-methylation; DNA damage; DR1533 locus; Genotoxic agents; Mn2+; SRA domain; Biophysics; Biochemistry; Molecular BiologyGenotoxic agents[SDV]Life Sciences [q-bio]DNA cytosine-methylationperspectiveSettore BIO/19 - Microbiologia GeneraleBiochemistrychemistry.chemical_compound0302 clinical medicineKanamycinCloning Molecularcytosine0303 health sciencesDR1533 locusbiologyChemistryGenotoxic agentuhrf1Mn(2+)Mn2+SRA domainDeinococcusrecognitionmanganese(ii)DNA BacterialDNA damageDNA repairoxidationUbiquitin-Protein LigasesBiophysicsSettore BIO/11 - Biologia Molecolareresistance03 medical and health sciencesBacterial ProteinsProtein DomainsDR1533 locuDrug Resistance BacterialEscherichia coliHumansfeaturesAmino Acid SequenceGeneMolecular Biology030304 developmental biologyOligonucleotideComputational BiologyDeinococcus radioduransDNA Methylationbiology.organism_classificationMolecular biologygenomic DNArepairMutationCCAAT-Enhancer-Binding ProteinsDNA damageHomologous recombination030217 neurology & neurosurgeryDNAGenome BacterialMutagens
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Molecular modes of action of cantharidin in tumor cells

2005

Cancer chemotherapy is often limited by patient's toxicity and tumor drug resistance indicating that new drug development and modification of existing drugs is critical for improving the therapeutic response. Traditional Chinese medicine is a rich source of potential anticancer agents. In particular, cantharidin (CAN), the active principle ingredient from the blister beetle, Mylabris, has anti-tumor activity, but the cytotoxic mechanism is unknown. In leukemia cells, cantharidin induces apoptosis by a p53-dependent mechanism. Cantharidin causes both DNA single- and double-strand breaks. Colony-forming assays with knockout and transfectant cells lines showed that DNA polymerase beta, but not…

DNA RepairDNA damageDNA repairBlister beetleAntineoplastic AgentsApoptosisDNA polymerase betaBiologyBiochemistrychemistry.chemical_compoundCell Line TumorHumansPharmacologyGeneticsCantharidinBase excision repairEndonucleasesbiology.organism_classificationDNA-Binding ProteinsOxidative StresschemistryCantharidinCancer researchERCC1DNA DamageNucleotide excision repairBiochemical Pharmacology
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Poly(ADP-ribosyl)ation accelerates DNA repair in a pathway dependent on Cockayne syndrome B protein

2003

Activation of poly(ADP-ribose)polymerases 1 and 2 (PARP-1 and PARP-2) is one of the earliest responses of mammalian cells to DNA damage by numerous genotoxic agents. We have analysed the influence of PARP inhibition, either achieved by over-expression of the DNA binding domain of PARP-1 or by treatment with 3,4-dihydro-5-[4-(1-piperidinyl)butoxyl]-1(2H)-isoquinolinone, on the repair of single-strand breaks (SSB), pyrimidine dimers and oxidative base modifications sensitive to Fpg protein (mostly 8-hydroxyguanine) in mammalian cells at very low, non-cytotoxic levels of DNA damage. The data show that the repair rates of all three types of DNA damage are significantly lower in PARP-inhibited c…

DNA RepairDNA damageDNA repairPoly ADP ribose polymerase[SDV]Life Sciences [q-bio]Pyrimidine dimerBiologyPoly(ADP-ribose) Polymerase InhibitorsPoly (ADP-Ribose) Polymerase InhibitorCockayne syndromeDexamethasone03 medical and health sciencesMice0302 clinical medicinePiperidinesCricetinaeGeneticsmedicineAnimalsPoly-ADP-Ribose Binding ProteinsComputingMilieux_MISCELLANEOUS030304 developmental biologyCell Line TransformedMice Knockout0303 health sciencesDNA HelicasesArticlesDNADNA repair protein XRCC4Fibroblastsmedicine.diseaseIsoquinolinesMolecular biology3. Good healthDNA Repair Enzymes030220 oncology & carcinogenesisPoly(ADP-ribose) PolymerasesNucleotide excision repairDNA DamageSignal Transduction
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Interaction with OGG1 Is Required for Efficient Recruitment of XRCC1 to Base Excision Repair and Maintenance of Genetic Stability after Exposure to O…

2015

International audience; XRCC1 is an essential protein required for the maintenance of genomic stability through its implication in DNA repair. The main function of XRCC1 is associated with its role in the single-strand break (SSB) and base excision repair (BER) pathways that share several enzymatic steps. We show here that the polymorphic XRCC1 variant R194W presents a defect in its interaction with the DNA glycosylase OGG1 after oxidative stress. While proficient for single-strand break repair (SSBR), this variant does not colocalize with OGG1, reflecting a defect in its involvement in BER. Consistent with a role of XRCC1 in the coordination of the BER pathway, induction of oxidative base …

DNA RepairDNA repairCHO CellsOxidative phosphorylation[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Biologymedicine.disease_causePolymorphism Single NucleotideDNA-binding proteinCell LineDNA GlycosylasesXRCC1Cricetulusmedicine[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]AnimalsHumansProtein Interaction Maps[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular Biology[SDV.BBM.BC] Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]GeneticsArticlesCell BiologyBase excision repairDNA-Binding ProteinsOxidative StressX-ray Repair Cross Complementing Protein 1DNA glycosylaseGene DeletionOxidative stressNucleotide excision repair
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Oxidative stress triggers the preferential assembly of base excision repair complexes on open chromatin regions

2010

How DNA repair machineries detect and access, within the context of chromatin, lesions inducing little or no distortion of the DNA structure is a poorly understood process. Removal of oxidized bases is initiated by a DNA glycosylase that recognises and excises the damaged base, initiating the base excision repair (BER) pathway. We show that upon induction of 8-oxoguanine, a mutagenic product of guanine oxidation, the mammalian 8-oxoguanine DNA glycosylase OGG1 is recruited together with other proteins involved in BER to euchromatin regions rich in RNA and RNA polymerase II and completely excluded from heterochromatin. The underlying mechanism does not require direct interaction of the prote…

DNA RepairHMG-boxDNA damageDNA repairGenome Integrity Repair and ReplicationCell LineDNA GlycosylasesEuchromatinDNA-(Apurinic or Apyrimidinic Site) LyaseGeneticsHumansGuanosinebiologyBromatesBase excision repairChromatinProliferating cell nuclear antigenChromatinDNA-Binding ProteinsOxidative StressX-ray Repair Cross Complementing Protein 1BiochemistryDNA glycosylasebiology.proteinDNA DamageNucleotide excision repairNucleic Acids Research
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Nucleotide excision repair of abasic DNA lesions

2019

AbstractApurinic/apyrimidinic (AP) sites are a class of highly mutagenic and toxic DNA lesions arising in the genome from a number of exogenous and endogenous sources. Repair of AP lesions takes place predominantly by the base excision pathway (BER). However, among chemically heterogeneous AP lesions formed in DNA, some are resistant to the endonuclease APE1 and thus refractory to BER. Here, we employed two types of reporter constructs accommodating synthetic APE1-resistant AP lesions to investigate the auxiliary repair mechanisms in human cells. By combined analyses of recovery of the transcription rate and suppression of transcriptional mutagenesis at specifically positioned AP lesions, w…

DNA RepairTranscription GeneticDNA damageDNA repairGenome Integrity Repair and ReplicationGene Knockout Techniques03 medical and health sciencesEndonucleasechemistry.chemical_compoundTranscription (biology)CRISPR-Associated Protein 9DNA-(Apurinic or Apyrimidinic Site) LyaseGeneticsHumansAP siteCell Line TransformedSkin030304 developmental biologyGene Editing0303 health sciencesBase SequencebiologyGenome Human030302 biochemistry & molecular biologyDNABase excision repairFibroblastsMolecular biologyXeroderma Pigmentosum Group A ProteinDNA-Binding ProteinschemistryMutationbiology.proteinCRISPR-Cas SystemsDNADNA DamageProtein BindingNucleotide excision repairNucleic Acids Research
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Cockayne syndrome: varied requirement of transcription-coupled nucleotide excision repair for the removal of three structurally different adducts fro…

2014

Hereditary defects in the transcription-coupled nucleotide excision repair (TC-NER) pathway of damaged DNA cause severe neurodegenerative disease Cockayne syndrome (CS), however the origin and chemical nature of the underlying DNA damage had remained unknown. To find out, to which degree the structural properties of DNA lesions determine the extent of transcription arrest in human CS cells, we performed quantitative host cell reactivation analyses of expression vectors containing various synthetic adducts. We found that a single 3-(deoxyguanosin-N 2-yl)-2-acetylaminofluorene adduct (dG(N 2)-AAF) constitutes an unsurmountable obstacle to transcription in both CS-A and CS-B cells and is remov…

DNA RepairTranscription GeneticGenetic ToxicologyDNA damagelcsh:MedicineBiologyToxicologyHost-Cell ReactivationBiochemistryCockayne syndromeCell LineDNA Adductschemistry.chemical_compoundGenes ReporterTranscription (biology)Nucleic AcidsMolecular Cell BiologyGene expressionmedicineHumansGene SilencingCockayne SyndromePoly-ADP-Ribose Binding Proteinslcsh:ScienceFluorenesMultidisciplinaryBiology and life sciencesOligonucleotidelcsh:RDNA HelicasesDeoxyguanosineDNACell Biologymedicine.diseaseMolecular biologyDNA Repair EnzymesGene Expression RegulationchemistryBiochemistrylcsh:QDNAResearch ArticleNucleotide excision repairPLoS ONE
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