Search results for "binding proteins"

showing 10 items of 911 documents

Identification of a novel activating mutation (Y842C) within the activation loop of FLT3 in patients with acute myeloid leukemia (AML).

2004

Fms-like tyrosine kinase 3 (FLT3) receptor mutations as internal tandem duplication (ITD) or within the kinase domain are detected in up to 35% of patients with acute myeloid leukemia (AML). N-benzoyl staurosporine (PKC412), a highly effective inhibitor of mutated FLT3 receptors, has significant antileukemic efficacy in patients with FLT3-mutated AML. Mutation screening of FLT3 exon 20 in AML patients (n = 110) revealed 2 patients with a novel mutation (Y842C) within the highly conserved activation loop of FLT3. FLT3-Y842C-transfected 32D cells showed constitutive FLT3 tyrosine phosphorylation and interleukin 3 (IL-3)-independent growth. Treatment with PKC412 led to inhibition of proliferat…

Models MolecularImmunologyBiologymedicine.disease_causeBiochemistryCell Linechemistry.chemical_compoundMicefluids and secretionshemic and lymphatic diseasesProto-Oncogene ProteinsmedicineSTAT5 Transcription FactorAnimalsHumansTyrosinePhosphotyrosineMutationCell CycleMyeloid leukemiaReceptor Protein-Tyrosine Kinaseshemic and immune systemsTyrosine phosphorylationCell BiologyHematologymedicine.diseaseMilk ProteinsProtein Structure TertiaryDNA-Binding ProteinsEnzyme ActivationLeukemiaLeukemia Myeloid AcutechemistryGene Expression Regulationfms-Like Tyrosine Kinase 3embryonic structuresFms-Like Tyrosine Kinase 3MutationCancer researchTrans-ActivatorsTyrosineSignal transductionTyrosine kinaseSignal TransductionBlood
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Structure of rat odorant-binding protein OBP1 at 1.6 angstrom resolution

2009

The nasal mucosa is a specialist interfacial region sandwiched between the olfactory system and the gaseous chemical milieu. In mammals and insects, this region is rich in odorant-binding proteins that are thought to aid olfaction by assisting mass transfer of the many different organoleptic compounds that make up the olfactory landscape. However, in mammals at least, our grasp on the exact function of odorant-binding proteins is tentative and better insight into the role of these proteins is warranted, not least because of their apparent significance in the olfactory systems of insects. Here, the crystal structure of rat odorant-binding protein 1 is reported at 1.6 Å resolution. This prote…

Models MolecularOlfactory systemCristallographyProtein ConformationRecombinant Fusion ProteinsMolecular Sequence DataOlfactionOBP1Crystallography X-RayReceptors Odorant010402 general chemistry01 natural sciencesPheromonesPichia pastoris03 medical and health sciences[ CHIM.CRIS ] Chemical Sciences/CristallographyProtein structureSpecies SpecificityStructural BiologyODORANT-BINDING PROTEINS[CHIM.CRIS]Chemical Sciences/CristallographyAnimalsAmino Acid SequencePeptide sequence030304 developmental biology0303 health sciencesBinding SitesSequence Homology Amino AcidbiologyProteinsGeneral MedicineLigand (biochemistry)biology.organism_classificationLipocalinsRatsCristallographie0104 chemical sciencesTransport proteinDNA-Binding ProteinsBiochemistryOdorant-binding proteinbiology.proteinODORANT-BINDING PROTEINS;OBP1Sequence Alignment
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Characterization of the pleiotropic LysR-type transcription regulator LeuO of Escherichia coli

2019

AbstractLeuO is a pleiotropic LysR-type transcriptional regulator (LTTR) and co-regulator of the abundant nucleoid-associated repressor protein H-NS in Gammaproteobacteria. As other LTTRs, LeuO is a tetramer that is formed by dimerization of the N-terminal DNA-binding domain (DBD) and C-terminal effector-binding domain (EBD). To characterize the Escherichia coli LeuO protein, we screened for LeuO mutants that activate the cas (CRISPR-associated/Cascade) promoter more effectively than wild-type LeuO. This yielded nine mutants carrying amino acid substitutions in the dimerization interface of the regulatory EBD, as shown by solving the EBD’s crystal structure. Superimposing of the crystal str…

Models MolecularProtein domainMutantRepressorPlasma protein bindingBiologymedicine.disease_cause03 medical and health sciencesProtein DomainsTranscription (biology)GeneticsConsensus sequencemedicinePromoter Regions GeneticEscherichia coli030304 developmental biologyGenetics0303 health sciences030306 microbiologyEscherichia coli ProteinsGene regulation Chromatin and EpigeneticsGenetic PleiotropyDNAGene Expression Regulation BacterialDNA-Binding ProteinsMutationNucleic Acid ConformationProtein MultimerizationDeoxyribonuclease IProtein BindingTranscription FactorsNucleic Acids Research
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Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
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Characterization of aCandida albicansgene encoding a putative transcriptional factor required for cell wall integrity

2003

After screening a Candida albicans genome database the product of an open reading frame (ORF) (CA2880) with 49% homology to the product of Saccharomyces cerevisiae YPL133c, a putative transcriptional factor, was identified. The disruption of the C. albicans gene leads to a major sensitivity to calcofluor white and Congo red, a minor sensitivity to sodium dodecyl sulfate, a major resistance to zymolyase, and an alteration of the chemical composition of the cell wall. For these reasons we called it CaCWT1 (for C. albicans cell wall transcription factor). CaCwt1p contains a putative Zn(II) Cys(6) DNA binding domain characteristic of some transcriptional factors and a PAS domain. The CaCWT1 gen…

Models MolecularTranscription GeneticGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeSequence HomologyMicrobiologyFungal ProteinsCell WallPAS domainGene Expression Regulation FungalCandida albicansGenes RegulatorGeneticsAmino Acid SequenceColoring AgentsCandida albicansMolecular BiologyGeneTranscription factorbiologyReverse Transcriptase Polymerase Chain ReactionGlucan Endo-13-beta-D-GlucosidaseComputational BiologySodium Dodecyl SulfateDNA-binding domainbiology.organism_classificationMolecular biologyCorpus albicansDNA-Binding ProteinsMutagenesis InsertionalOpen reading frameGenome FungalGene DeletionTranscription FactorsFEMS Microbiology Letters
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The 5' Untranslated Region of the

2018

Many of the virulence traits that make Candida albicans an important human fungal pathogen are regulated on a transcriptional level. Here, we report an important regulatory contribution of translation, which is exerted by the extensive 5′ untranslated regulatory sequence (5′ UTR) of the transcript for the protein Efg1, which determines growth, metabolism, and filamentation in the fungus. The presence of the 5′ UTR is required for efficient translation of Efg1, to promote filamentation. Because transcripts for many relevant regulators contain extensive 5′ UTR sequences, it appears that the virulence of C. albicans depends on the combination of transcriptional and translational regulatory mec…

Molecular Biology and PhysiologyDNA Mutational AnalysisEFG1Hyphaehyphal morphogenesisGene Expressiontranslationposttranscriptional regulationDNA-Binding ProteinsFungal Proteinsfilamentation5′ UTRGenes ReporterPolyribosomesProtein BiosynthesisCandida albicansMorphogenesisHumans5' Untranslated RegionsTranscription FactorsResearch ArticlemSphere
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Deciphering the Rules Underlying Xenogeneic Silencing and Counter-Silencing of Lsr2-like Proteins Using CgpS of Corynebacterium glutamicum as a Model

2020

In actinobacteria, Lsr2-like nucleoid-associated proteins function as xenogeneic silencers (XS) of horizontally acquired genomic regions, including viral elements, virulence gene clusters in Mycobacterium tuberculosis, and genes involved in cryptic specialized metabolism in Streptomyces species. Consequently, a detailed mechanistic understanding of Lsr2 binding in vivo is relevant as a potential drug target and for the identification of novel bioactive compounds. Here, we followed an in vivo approach to investigate the rules underlying xenogeneic silencing and counter-silencing of the Lsr2-like XS CgpS from Corynebacterium glutamicum. Our results demonstrated that CgpS distinguishes between…

Molecular Biology and PhysiologyGene Transfer HorizontalactinobacteriaMicrobiologyQR1-502Corynebacterium glutamicumDNA-Binding Proteinsregulatory networksBacterial Proteinslsr2ddc:570xenogeneic silencinghorizontal gene transferGene Silencingcounter-silencingat-rich dnaProtein BindingTranscription FactorsResearch ArticlemBio
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The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

1997

The psychrotrophic bacterium Pseudomonas fragi was subjected to cold shocks from 30 or 20 to 5 degrees C. The downshifts were followed by a lag phase before growth resumed at a characteristic 5 degrees C growth rate. The analysis of protein patterns by two-dimentional gel electrophoresis revealed overexpression of 25 or 17 proteins and underexpression of 12 proteins following the 30- or 20-to-5 degrees C shift, respectively. The two downshifts shared similar variations of synthesis of 20 proteins. The kinetic analysis distinguished the induced proteins into cold shock proteins (Csps), which were rapidly but transiently overexpressed, and cold acclimation proteins (Caps), which were more or …

Molecular Sequence DataAdaptation BiologicalBiologyMicrobiologyPolymerase Chain Reaction03 medical and health sciencesHeat acclimationBacterial ProteinsPseudomonas fragiHeat shock proteinNucleic AcidsPseudomonasCold acclimationElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequence[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyHeat-Shock ProteinsComputingMilieux_MISCELLANEOUS030304 developmental biologyGel electrophoresis0303 health sciencesBase SequenceSequence Homology Amino Acid030306 microbiologySequence Analysis DNACold-shock domainbiology.organism_classificationMolecular biologyCold shock responseCold TemperatureDNA-Binding Proteins[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryGenes BacterialCarrier ProteinsSequence AnalysisGenome BacterialResearch ArticleProtein Binding
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Molecular characterization of the zerknüllt region of the Antennapedia complex of D. subobscura.

1995

We have characterized at the molecular level the zerknullt (zen) region of the Drosophila subobscura Antennapedia complex. The sequence comparison between D. subobscura and D. melanogaster shows an irregular distribution of the conserved and diverged regions, with the homeobox and a putative activating domain completely conserved. Comparisons of the promoter sequence and pattern of expression of the gene during development suggest that the regulation of zen has been conserved during evolution. The conservation of zen expression in a subpopulation of the polar cells indicates the existence of an important role in such cells. We describe a transitory segmented pattern of expression of zen in …

Molecular Sequence DataPair-rule geneGenes InsectAntennapediaGenomeChromosomesGeneticsMelanogasterAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerCloning MolecularPromoter Regions GeneticGeneGenetics (clinical)In Situ HybridizationGeneticsHomeodomain ProteinsbiologyBase SequencefungiGenes HomeoboxChromosomeChromosome MappingGene Expression Regulation DevelopmentalNuclear Proteinsbiology.organism_classificationDrosophila subobscuraDNA-Binding ProteinsRepressor ProteinsInsect HormonesAntennapedia Homeodomain ProteinHomeoboxDrosophilaSequence AlignmentTranscription FactorsChromosoma
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Engineering a 2D protein-DNA crystal.

2005

(Figure Presented) Weaving with DNA: A DNA-binding protein was used to control the structure of a self-assembled 2D crystal. In the absence of protein, four oligonucleotides hybridize to form a Kagome lattice of interwoven double helices with p3 symmetry (see image). Addition of protein RuvA during assembly changes the symmetry and connectivity to give a DNA-protein crystal with an approximately square unit cell. © 2005 Wiley-VCH Verlag GmbH and Co. KGaA.

Molecular Sequence DataProtein dnaPlasma protein bindingCatalysislaw.inventionCrystalNucleic acid thermodynamicschemistry.chemical_compoundlawNanotechnologyBase sequenceCrystallizationOligonucleotide Array Sequence AnalysisDNA CruciformBase SequenceEscherichia coli ProteinsDNA HelicasesNucleic Acid HybridizationGeneral MedicineDNAGeneral ChemistryDNA-Binding ProteinsMicroscopy ElectronCrystallographychemistryBiochemistryCrystallizationDNAProtein BindingAngewandte Chemie (International ed. in English)
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