Search results for "Transferase"

showing 10 items of 1030 documents

Knockout of myeloid cell leukemia-1 induces liver damage and increases apoptosis susceptibility of murine hepatocytes

2008

Apoptosis, or programmed cell death, regulates tissue development and homeostasis in multi-cellular organisms. Extrinsic or intrinsic death signals activate pro-apoptotic pathways, resulting in the activation of caspases and finally in cell death. An important event during apoptosis process is the permeabilization of the outer mitochondrial membrane (OMM). Integrity of the OMM is regulated by the Bcl-2 protein family, which is divided into three groups: anti-apoptotic members Bcl-2, Bcl-xL and myeloid cell leukemia-1 (Mcl-1), pro-apoptotic multidomain members Bax and Bak, and pro-apoptotic BH3-only proteins. Mitochondrial activation is regulated by selective interactions of Bcl-2 proteins v…

Programmed cell deathGenotypeCellular differentiation610 Medicine & healthApoptosisBiologyPolymerase Chain ReactionArticleMiceimmune system diseases10049 Institute of Pathology and Molecular Pathologyhemic and lymphatic diseasesmedicineAnimalsAspartate AminotransferasesneoplasmsDNA PrimersHepatologyCaspase 3Alanine TransaminaseCell DifferentiationDNAFas receptorCell biologyMyeloid Cell Leukemia Sequence 1 ProteinHaematopoiesisGene Expression RegulationLiverProto-Oncogene Proteins c-bcl-2ApoptosisHepatocytesMyeloid Cell Leukemia Sequence 1 ProteinRNA2721 HepatologyHepatocyte growth factorStem cellmedicine.drugHepatology
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Brca2/Xrcc2 dependent HR, but not NHEJ, is required for protection against O6-methylguanine triggered apoptosis, DSBs and chromosomal aberrations by …

2008

Abstract O 6 -methylguanine (O 6 MeG) is a highly critical DNA adduct induced by methylating carcinogens and anticancer drugs such as temozolomide, streptozotocine, procarbazine and dacarbazine. Induction of cell death by O 6 MeG lesions requires mismatch repair (MMR) and cell proliferation and is thought to be dependent on the formation of DNA double-strand breaks (DSBs) or, according to an alternative hypothesis, direct signaling by the MMR complex. Given a role for DSBs in this process, either homologous recombination (HR) or non-homologous end joining (NHEJ) or both might protect against O 6 MeG. Here, we compared the response of cells mutated in HR and NHEJ proteins to temozolomide and…

Programmed cell deathGuanineKu80DNA RepairDown-RegulationFluorescent Antibody TechniqueApoptosisCHO CellsBiologyTransfectionBiochemistryMiceO(6)-Methylguanine-DNA MethyltransferaseCricetulusCricetinaeDNA adductTemozolomideAnimalsDNA Breaks Double-StrandedMolecular BiologyBRCA2 ProteinChromosome AberrationsRecombination GeneticCell DeathCell growthCell BiologyTransfectionCell cycleMolecular biologyDNA-Binding ProteinsDacarbazineApoptosisMutationCancer researchHomologous recombinationSister Chromatid ExchangeDNA Repair
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Evolutionary and structural analyses of GDAP1, involved in Charcot-Marie-Tooth disease, characterize a novel class of glutathione transferase-related…

2003

Mutations in the Ganglioside-induced differentiation-associated protein-1 (GDAP1) gene cause autosomal recessive Charcot-Marie-Tooth disease type 4A. The protein encoded by GDAP1 shows clear similarity to glutathione transferases (also known as glutathione S-transferases or GSTs). The human genome contains a paralog of GDAP1 called GDAP1L1. Using comparative genomics, we show that orthologs of GDAP1 and GDAP1L1 are found in mammals, birds, amphibians, and fishes. Likely orthologs of those genes in invertebrates and a low but consistent similarity with some plant and eubacterial genes have also been found. We demonstrate that GDAP1 and GDAP1L1 do not belong to any of the known classes of GST…

Protein ConformationMolecular Sequence DataSequence alignmentNerve Tissue ProteinsBiologyEvolution MolecularProtein structurePhylogeneticsCharcot-Marie-Tooth DiseaseDatabases GeneticGeneticsCluster AnalysisHumansAmino Acid SequenceMolecular BiologyPeptide sequenceGeneEcology Evolution Behavior and SystematicsPhylogenyGlutathione TransferaseComparative genomicsGeneticsTransmembrane domainMultigene FamilyHuman genomeSequence AlignmentMolecular biology and evolution
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Two amino acid residues determine the low substrate affinity of human cationic amino acid transporter-2A.

2003

Mammalian cationic amino acid transporters (CAT) differ in their substrate affinity and sensitivity to trans-stimulation. The apparent Km values for cationic amino acids and the sensitivity to trans-stimulation of CAT-1, -2B, and -3 are characteristic of system y+. In contrast, CAT-2A exhibits a 10-fold lower substrate affinity and is largely independent of substrate at the trans-side of the membrane. CAT-2A and -2B demonstrate such divergent transport properties, even though their amino acid sequences differ only in a stretch of 42 amino acids. Here, we identify two amino acid residues within this 42-amino acid domain of the human CAT-2A protein that are responsible for the apparent low af…

Protein ConformationRecombinant Fusion ProteinsBlotting WesternGreen Fluorescent ProteinsMolecular Sequence DataGene ExpressionArginineTransfectionBiochemistryStructure-Activity RelationshipXenopus laevisExtracellularAnimalsHumansBiotinylationAmino acid transporterAmino Acid SequenceAmino AcidsCationic Amino Acid Transporter 2Molecular BiologyGlutathione Transferasechemistry.chemical_classificationBinding SitesSubstrate (chemistry)Biological TransportCell BiologyPhoto-reactive amino acid analogAmino acidTransmembrane domainLuminescent ProteinsS-tagchemistryBiochemistryMutagenesis Site-DirectedOocytesElectrophoresis Polyacrylamide GelFemaleIntracellularThe Journal of biological chemistry
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The cytosolic Arabidopsis thaliana cysteine desulfurase ABA3 delivers sulfur to the sulfurtransferase STR18

2020

ABSTRACTThe biosynthesis of many sulfur-containing molecules depends on cysteine as a sulfur source. Cysteine desulfurase (CD) and rhodanese (Rhd) domain-containing protein families participate in the trafficking of sulfur for various metabolic pathways in bacteria and human, but their connection is not yet described in plants. The existence of natural chimeric proteins, however, containing both CD and Rhd domains in specific bacterial genera suggests a general interaction between both proteins. We report here the biochemical relationships between two cytosolic proteins from Arabidopsis thaliana, a Rhd domain containing protein, the sulfurtransferase 18 (STR18), and a CD isoform referred to…

Protein familyArabidopsisSulfurtransferaseRhodaneseBiochemistry03 medical and health scienceschemistry.chemical_compoundCytosolProtein DomainsArabidopsis thalianaCysteineMolecular Biology030304 developmental biology0303 health sciencesbiologyArabidopsis ProteinsCysteine desulfurase030302 biochemistry & molecular biologyCell Biologybiology.organism_classificationFusion proteinThiosulfate SulfurtransferaseCarbon-Sulfur LyasesBiochemistrychemistrySulfurtransferasesMolybdenum cofactorSulfurCysteine
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LASS6, an additional member of the longevity assurance gene family

2005

Longevity assurance genes (LAGs) represent a subgroup of the homeobox gene family. Five mammalian homologs have been reported, and the corresponding proteins have previously been investigated with respect to their key role in ceramide synthesis. However, members of the LAG family have been shown to be involved in cell growth regulation and cancer differentiation. In an effort to characterize additional members of the LAG family, we have screened the latest releases of genomic databases and report on the bioinformatic characterization of yet another member, LAG1 longevity assurance homolog 6 (LASS6). Like other LAG family members, the LASS6 protein contained a homeodomain and LAG1 domain. In…

Protein familyProtein ConformationIn silicoLongevityMolecular Sequence DataBiologyHomology (biology)MiceDatabases GeneticSphingosine N-AcyltransferaseGeneticsAnimalsHumansGene familyAmino Acid SequenceGeneZebrafishPhylogenyZebrafishHomeodomain ProteinsGeneticsBase SequenceGenome HumanMicroarray analysis techniquesGenes HomeoboxMembrane ProteinsGeneral Medicinebiology.organism_classificationRatsChromosomes Human Pair 2HomeoboxInternational Journal of Molecular Medicine
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A Survey on Tubulin and Arginine Methyltransferase Families Sheds Light on

2019

Tubulins and microtubules (MTs) represent targets for taxane-based chemotherapy. To date, several lines of evidence suggest that effectiveness of compounds binding tubulin often relies on different post-translational modifications on tubulins. Among them, methylation was recently associated to drug resistance mechanisms impairing taxanes binding. The sea urchin is recognized as a research model in several fields including fertilization, embryo development and toxicology. To date, some α- and β-tubulin genes have been identified in P. lividus, while no data are available in echinoderms for arginine methyl transferases (PRMT). To evaluate the exploiting of the sea urchin embryo in the field o…

Protein-Arginine N-MethyltransferasesEmbryo NonmammalianPRMTechinodermsIntracellular Signaling Peptides and Proteinsmacromolecular substancesCytostatic AgentsMethylationTubulin ModulatorsArticlearginine methylationsea urchintubulinpost-translational modificationSea Urchinsembryonic structuresToxicity TestsAnimalsProtein Processing Post-TranslationalInternational journal of molecular sciences
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A TR-FRET based functional assay for screening activators of CARM1

2013

Epigenome is an emerging field that demands selective cell-permeable chemical probes to perturb, especially in vivo, the activity of specific enzymes involved in modulating the epigenetic codes. Coactivator Associated Arginine (R) Methyltransferase 1 (CARM1) is a coactivator of estrogen receptor α (ERα), the main target in human breast cancer. We previously showed that overexpression of CARM1 by two-fold in MCF7 breast cancer cells increased the expression of ERα-target genes involved in differentiation and reduced cell proliferation, leading to the hypothesis that activating CARM1 by chemical activators may be therapeutically effective in breast cancer. Selective, potent, cell-permeable CA…

Protein-Arginine N-MethyltransferasesTime FactorsCARM1CARM1; arginine; FRET; methylation; PABP1High-throughput screeningEstrogen receptorarginineBacMamBreast NeoplasmsBiologyBiochemistryArticleEnzyme activatorCoactivatorFluorescence Resonance Energy TransferHumansEpigeneticsPABP1Molecular BiologyOrganic ChemistryFusion proteinEnzyme ActivationCARM1BiochemistryFRETMCF-7 CellsMolecular MedicineFemalemethylation
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Proteome analysis and identification of symbiosis-related proteins from Medicago truncatula Gaertn. by two-dimensional electrophoresis and mass spect…

2002

Time-course analysis of root protein profiles was studied by two-dimensional gel electrophoresis and silver staining in the model plant Medicago truncatula, inoculated either with the arbuscular mycorrhizal fungus Glomus mosseae or with the nitrogen fixing bacterium Sinorhizobium meliloti. Protein modifications in relation to the development of both symbioses included down- and upregulations, as well as newly induced polypeptides. Matrix assisted laser desorption/ionization-time of flight-mass spectrometry after trypsin digestion clearly identified one polypeptide induced in nodulated roots as a M. truncatula leghemoglobin. Internal sequencing with a quadrupole time-of-flight mass spectrome…

Proteome[SDV]Life Sciences [q-bio]Clinical BiochemistryMass spectrometryBiochemistryMass SpectrometryAnalytical ChemistryGene Expression Regulation PlantBotanyMedicagoElectrophoresis Gel Two-DimensionalLeghemoglobinSymbiosisGlomusComputingMilieux_MISCELLANEOUSPlant ProteinsGel electrophoresisSinorhizobium melilotibiologyfungiFungifood and beveragesbiology.organism_classificationMedicago truncatula[SDV] Life Sciences [q-bio]BiochemistrySerine hydroxymethyltransferaseProteomeSinorhizobium melilotiElectrophoresis
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Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.

2014

Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification…

ProteomicsSaccharomyces cerevisiae Proteinslcsh:QH426-470Saccharomyces cerevisiaeBiochemistryMolecular GeneticsRNA TransferGene Expression Regulation FungalMolecular Cell BiologyGeneticsFungal GeneticsPhosphorylationPost-Translational ModificationUridineMolecular BiologyAdaptor Proteins Signal TransducingHistone AcetyltransferasesAlanineSpectrometric Identification of ProteinsBiology and life sciencesCasein Kinase INucleotidesMicrobial GeneticsProteinsCell BiologyPeptide Elongation Factorslcsh:GeneticsPhenotypeMultiprotein ComplexesRNAMolecular ComplexesTransfer RNAAnticodonsResearch ArticlePLoS genetics
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