Search results for "BINDING DOMAIN"

showing 10 items of 81 documents

RNA-binding activity of the rat calmodulin-binding PEP-19 protein and of the long PEP-19 isoform

2012

Synthesis of H1˚ histone protein, in the developing rat brain, seems to be regulated mainly at the post-transcriptional level. Since regulation of RNA metabolism depends on a series of RNA-binding proteins, we have been searching for RNA-binding proteins involved in the post-transcriptional regulation of the H1˚ gene. We recently reported isolation, from a cDNA expression library, of an insert encoding a novel protein, the C-terminal half of which is identical to that of PEP-19, a brain-specific protein involved in calcium metabolism. The novel protein was called long PEP-19 isoform (LPI). Herein we show that LPI, as well as PEP-19, can bind H1˚ RNA. Moreover, in order to improve production…

Gene isoformCalmodulinCalmodulin binding domainNerve Tissue ProteinsRNA-binding proteinRNA-binding proteins histone variants H1˚ PEP-19 long PEP-19 isoform calmodulinBiologyBinding CompetitiveRats Sprague-DawleyCalmodulinGeneticsAnimalsProtein IsoformsE2F1RNA Processing Post-TranscriptionalGeneHistidineRNA-Binding ProteinsRNAGeneral MedicineMolecular biologyRatsBiochemistrybiology.proteinRNACalmodulin-Binding ProteinsProtein BindingInternational Journal of Molecular Medicine
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Methyl-CpG-binding proteins

2000

CpG methylation, the most common epigenetic modification of vertebrate genomes, is primarily associated with transcriptional repression. MeCP2, MBD1, MBD2, MBD3 and MBD4 constitute a family of vertebrate proteins that share the methyl-CpG-binding domain (MBD). The MBD, consisting of about 70 residues, possesses a unique alpha/beta-sandwich structure with characteristic loops, and is able to bind single methylated CpG pairs as a monomer. All MBDs except MBD4, an endonuclease that forms a complex with the DNA mismatch-repair protein MLH1, form complexes with histone deacetylase. It has been established that MeCP2, MBD1 and MBD2 are involved in histone deacetylase-dependent repression and it i…

GeneticsTranscription GeneticChromosomal Proteins Non-HistoneMethyl-CpG-Binding Protein 2Molecular Sequence DataDNADNA MethylationBiologyBiochemistryProtein Structure TertiaryMethyl-CpG-binding domainDNA-Binding ProteinsRepressor ProteinsEpigenetics of physical exerciseHistone methyltransferaseDNA methylationHistone methylationHistone H2AAnimalsHumansHistone codeCpG IslandsAmino Acid SequenceGene SilencingCancer epigeneticsEuropean Journal of Biochemistry
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A Major Effect Gene Controlling Development and Pathogenicity in Botrytis cinerea Identified Through Genetic Analysis of Natural Mycelial Non-pathoge…

2021

Botrytis cinerea is a necrotrophic plant pathogenic fungus with a wide host range. Its natural populations are phenotypically and genetically very diverse. A survey of B. cinerea isolates causing gray mold in the vineyards of Castilla y León, Spain, was carried out and as a result eight non-pathogenic natural variants were identified. Phenotypically these isolates belong to two groups. The first group consists of seven isolates displaying a characteristic mycelial morphotype, which do not sporulate and is unable to produce sclerotia. The second group includes one isolate, which sporulates profusely and does not produce sclerotia. All of them are unresponsive to light. Crosses between a repr…

Geneticsgray moldBulked segregant analysisLocus (genetics)bulked segregant analysiPlant SciencePathogenic fungusBiologylcsh:Plant cultureacetyl transferasebiology.organism_classificationGenetic analysisLaboratorium voor PhytopathologieDNA binding domainComplementationbulked segregant analysisLaboratory of Phytopathologygenetic complementationlcsh:SB1-1110AlleleEPSGeneBotrytis cinereaOriginal ResearchFrontiers in Plant Science
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New point mutation (R243W) in the hormone binding domain of the c‐erbA β1 gene in a family with generalized resistance to thyroid hormone

1996

Two years after the first mutation on exon 7 in the carboxy-terminal part of the hinge domain (D) was reported (Behr and Loos 1992), we have identified the second mutation on exon 7 in patients with GRTH. Interestingly, our mutation it is not located in the two previously described "hot spot regions", but instead very close to the hinge domain (D) of the receptor protein that is essential for the function of the hormone binding domain (E) (Lin et al., 1991). Confirming the observation that the majority of single base substitutions causing human genetic diseases or DNA polymorphisms follow the hot spot mutation rule of CG to TG and CG to CA transition (Barker et al., 1984), an additional CpG…

Geneticsmedicine.medical_specialtyThyroid hormone receptorPoint mutationBiologyThyroid hormone receptor betaExonEndocrinologyCpG siteInternal medicinemedicineGeneticsReceptorGeneGenetics (clinical)Binding domainHuman Mutation
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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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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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Mutations in DNA Binding and Transactivation Domains Affect the Dynamics of Parvovirus NS1 Protein

2013

ABSTRACT The multifunctional replication protein of autonomous parvoviruses, NS1, is vital for viral genome replication and for the control of viral protein production. Two DNA-interacting domains of NS1, the N-terminal and helicase domains, are necessary for these functions. In addition, the N and C termini of NS1 are required for activation of viral promoter P38. By comparison with the structural and biochemical data from other parvoviruses, we identified potential DNA-interacting amino acid residues from canine parvovirus NS1. The role of the identified amino acids in NS1 binding dynamics was studied by mutagenesis, fluorescence recovery after photobleaching, and computer simulations. Mu…

HMG-boxParvovirus CaninevirusesImmunologyDNA Mutational AnalysisMutation MissenseNS1 proteiiniViral Nonstructural ProteinsVirus ReplicationMicrobiologyNS1 proteinSingle-stranded binding proteinCell LineSeqA protein domainVirologyAnimalsDNA bindingReplication protein AbiologyTer proteinparvovirusvirus diseasesDNAn sitoutuminen [DNA]biochemical phenomena metabolism and nutritionMolecular biologyCell biologyVirus-Cell InteractionsProtein Structure TertiaryDNA binding siteDNA-Binding ProteinsInsect Sciencebiology.proteinMutant ProteinsViral genome replicationBinding domainProtein Binding
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Structure and function of the vacuolar Ccc1/VIT1 family of iron transporters and its regulation in fungi

2020

Iron is an essential micronutrient for most living beings since it participates as a redox active cofactor in many biological processes including cellular respiration, lipid biosynthesis, DNA replication and repair, and ribosome biogenesis and recycling. However, when present in excess, iron can participate in Fenton reactions and generate reactive oxygen species that damage cells at the level of proteins, lipids and nucleic acids. Organisms have developed different molecular strategies to protect themselves against the harmful effects of high concentrations of iron. In the case of fungi and plants, detoxification mainly occurs by importing cytosolic iron into the vacuole through the Ccc1/V…

ISC Iron-sulfur lusterCS Consistency scoreCcc1Ribosome biogenesisVacuoleReview ArticleYRE Yap response elementsBiochemistryBiotecnologia0302 clinical medicineStructural BiologyCg Candida glabrata0303 health sciencesMAFFT Multiple Alignment using Fast Fourier TransformNRAMP Natural Resistance-Associated Macrophage ProteinbiologyVIT1ChemistryMBD Metal-binding domainPlantsComputer Science ApplicationsBiochemistry030220 oncology & carcinogenesisCRD Cysteine-rich domainEg Eucalyptus grandisIron detoxificationBiotechnologyCBC CCAAT-binding core complexlcsh:BiotechnologySaccharomyces cerevisiaeVTL Vacuolar iron transporter-likeBiophysicsVIT Vacuolar iron transporterbZIP basic leucine-zipper03 medical and health sciencesFongsLipid biosynthesislcsh:TP248.13-248.65GeneticsFe IronIron transportTranscription factor030304 developmental biologyComputingMethodologies_COMPUTERGRAPHICSBLOSUM BLOcks SUbstitution MatrixTMD Transmembrane domainML Maximum-likelihoodIron regulationDNA replicationFungibiology.organism_classificationYeastYeastMetabolic pathwayH HelixHap Heme activator proteinVacuoleROS Reactive oxygen speciesFerroComputational and Structural Biotechnology Journal
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Isolation and Characterization of the Kininogen-binding Protein p33 from Endothelial Cells

1996

Abstract Kininogens, the precursor proteins of the vasoactive kinins, bind specifically, reversibly, and saturably to platelets, neutrophils, and endothelial cells. Two domains of the kininogens expose major cell binding sites: domain D3 that is shared by H- and L-kininogen and domain D5H that is exclusively present in H-kininogen. Previously we have mapped the kininogen cell binding sites to 27 residues of D3 (“LDC27”) and 20 residues of D5H (“HKH20”), respectively (Herwald, H., Hasan, A. A. K., Godovac-Zimmermann, J., Schmaier, A. H., and Muller-Esterl, W. (1995) J. Biol. Chem. 270, 14634-14642; Hasan, A. A. K., Cines, D. B., Herwald, H., Schmaier, A. H., and Muller-Esterl, W. (1995) J. B…

Kininogen bindingchemistry.chemical_classificationFactor XIIKininogenBinding proteinPrekallikreinPeptideCell BiologyBiologyBiochemistryMolecular biologyBiochemistryAffinity chromatographychemistryMolecular Biologycirculatory and respiratory physiologyBinding domainJournal of Biological Chemistry
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Quantification of the Raf-C1 Interaction With Solid-Supported Bilayers

2002

By use of the quartz crystal microbalance technique, the interaction of the Raf-Ras binding domain (RafRBD) and the cysteine-rich domain Raf-C1 with lipids was quantified by using solid-supported bilayers immobilized on gold electrodes deposited on 5 MHz quartz plates. Solid-supported lipid bilayers were composed of an initial octanethiol monolayer chemisorbed on gold and a physisorbed phospholipid monolayer varying in its lipid composition as the outermost layer. The integrity of bilayer preparation was monitored by impedance spectroscopy. For binding experiments, a protein construct comprising the RafRBD and Raf-C1 linked to the maltose binding protein and a His tag, termed MBP-Raf-C1, wa…

Lipid BilayersPhospholipidBiosensing TechniquesMicroscopy Atomic ForceBiochemistrychemistry.chemical_compoundMonolayerLipid bilayerMolecular BiologyBilayerOrganic ChemistryUnithiolQuartz crystal microbalanceProtein Structure TertiaryProto-Oncogene Proteins c-rafDissociation constantCrystallographychemistryThermodynamicsMolecular Medicinelipids (amino acids peptides and proteins)AdsorptionGoldDimyristoylphosphatidylcholineProtein adsorptionBinding domainChemBioChem
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