Search results for "Mutant Proteins"

showing 10 items of 24 documents

Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and …

2016

The IM30 (inner membrane-associated protein of 30 kDa), also known as the Vipp1 (vesicle-inducing protein in plastids 1), has a crucial role in thylakoid membrane biogenesis and maintenance. Recent results suggest that the protein binds peripherally to membranes containing negatively charged lipids. However, although IM30 monomers interact and assemble into large oligomeric ring complexes with different numbers of monomers, it is still an open question whether ring formation is crucial for membrane interaction. Here we show that binding of IM30 rings to negatively charged phosphatidylglycerol membrane surfaces results in a higher ordered membrane state, both in the head group and in the inn…

0301 basic medicineChloroplastsMembrane lipids02 engineering and technologyBiologyBiochemistryThylakoids03 medical and health scienceschemistry.chemical_compoundMembrane LipidsBacterial ProteinsMembrane BiologyLipid bilayerProtein Structure QuaternaryMolecular BiologyPhosphatidylglycerolSynechocystisMembrane ProteinsBiological membranePhosphatidylglycerolsCell BiologySurface Plasmon Resonance021001 nanoscience & nanotechnologyKinetics030104 developmental biologyMembranechemistryBiochemistryMembrane proteinThylakoidMembrane biogenesisBiophysicsMutant ProteinsProtein Multimerization0210 nano-technologyProtein BindingThe Journal of biological chemistry
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Apoptotic Activity of MeCP2 Is Enhanced by C-Terminal Truncating Mutations.

2016

Methyl-CpG binding protein 2 (MeCP2) is a widely abundant, multifunctional protein most highly expressed in post-mitotic neurons. Mutations causing Rett syndrome and related neurodevelopmental disorders have been identified along the entire MECP2 locus, but symptoms vary depending on mutation type and location. C-terminal mutations are prevalent, but little is known about the function of the MeCP2 C-terminus. We employ the genetic efficiency of Drosophila to provide evidence that expression of p.Arg294* (more commonly identified as R294X), a human MECP2 E2 mutant allele causing truncation of the C-terminal domains, promotes apoptosis of identified neurons in vivo. We confirm this novel find…

0301 basic medicineMethyl-CpG-Binding Protein 2lcsh:MedicineApoptosisBiochemistryPhosphoserine0302 clinical medicineAnimal CellsDrosophila ProteinsPost-Translational ModificationPhosphorylationlcsh:ScienceNeuronsMotor NeuronsGeneticsMultidisciplinaryCell DeathbiologyDrosophila MelanogasterAnimal ModelsInsectsFOXG1Cell ProcessesCaspasesPhosphorylationDrosophilaBiological CulturesCellular TypesDrosophila melanogasterResearch ArticleGene isoformcongenital hereditary and neonatal diseases and abnormalitiesArthropodaProtein domainMouse ModelsMotor ActivityResearch and Analysis MethodsTransfectionModels BiologicalMECP203 medical and health sciencesModel OrganismsProtein Domainsmental disordersAnimalsHumansMolecular Biology TechniquesImmunohistochemistry TechniquesMolecular BiologyTranscription factorBinding proteinlcsh:ROrganismsBiology and Life SciencesProteinsCell BiologyCell Culturesbiology.organism_classificationInvertebratesHistochemistry and Cytochemistry TechniquesHEK293 Cells030104 developmental biologyCellular NeuroscienceMutationImmunologic TechniquesMutant Proteinslcsh:Q030217 neurology & neurosurgeryNeuroscienceTranscription FactorsPLoS ONE
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Protein aggregation in congenital myopathies.

2011

Protein aggregation in congenital myopathies may be encountered among different myofibrillar myopathies such as granulofilamentous myopathy, cytoplasmic body myopathy, or spheroid body myopathy, which are designated as αB crystallinopathy, desminopathy, and myotilinopathy, respectively, according to the respective mutant proteins. Caps in cap disease and reducing bodies in reducing body myopathy were disclosed to contain numerous proteins. The multitude of diverse proteins aggregating within muscle fibers suggests impaired extralysosomal degradation of proteins, a disturbance of catabolism. The lack of different proteins accruing, but the mutant ones at an early age of affected patients in …

AdultCatabolismMutantInfantProtein aggregationBiologySarcomereActinsDesminBiochemistryChild PreschoolPediatrics Perinatology and Child HealthMyosinMutationmedicineHumansMutant ProteinsNeurology (clinical)medicine.symptomMyopathyMyofibrilChildActinMyopathies Structural CongenitalSeminars in pediatric neurology
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A new PCSK9 gene promoter variant affects gene expression and causes autosomal dominant hypercholesterolemia.

2008

Autosomal dominant hypercholesterolemia (ADH) is a genetic disorder characterized by increased low-density lipoprotein (LDL)-cholesterol levels, leading to high risk of premature cardiovascular disease. More than 900 mutations in LDL receptor, six in APOB and 10 in PCSK9 have been identified as a cause of the disease in different populations. All known mutations in PCSK9 causing hypercholesterolemia produce an increase in the enzymatic activity of this protease. Up to now, there are data about the implication of PCSK9 in ADH in a low number of populations, not including a Spanish population.The objective of the study was to study the prevalence of PCSK9 mutations in ADH Spanish population.W…

Adultmedicine.medical_specialtyApolipoprotein BEndocrinology Diabetes and MetabolismClinical BiochemistryGene ExpressionTransfectionBiochemistryPolymorphism Single NucleotideHyperlipoproteinemia Type IIPCSK9 GeneMiceEndocrinologyGene FrequencyInternal medicinemedicineAnimalsHumansPromoter Regions GeneticAllele frequencyGeneCells CulturedGeneticsbiologyBase SequencePCSK9Biochemistry (medical)Serine EndopeptidasesGenetic disorderHyperlipoproteinemia Type IIaMiddle Agedmedicine.diseaseEndocrinologySpainCase-Control StudiesLDL receptorbiology.proteinNIH 3T3 Cellslipids (amino acids peptides and proteins)Mutant ProteinsProprotein ConvertasesProprotein Convertase 9The Journal of clinical endocrinology and metabolism
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Cyclopropanation of Membrane Unsaturated Fatty Acids Is Not Essential to the Acid Stress Response of Lactococcus lactis subsp. cremoris

2011

ABSTRACT Cyclopropane fatty acids (CFAs) are synthetized in situ by the transfer of a methylene group from S -adenosyl- l -methionine to a double bond of unsaturated fatty acid chains of membrane phospholipids. This conversion, catalyzed by the Cfa synthase enzyme, occurs in many bacteria and is recognized to play a key role in the adaptation of bacteria in response to a drastic perturbation of the environment. The role of CFAs in the acid tolerance response was investigated in the lactic acid bacterium Lactococcus lactis MG1363. A mutant of the cfa gene was constructed by allelic exchange. The cfa gene encoding the Cfa synthase was cloned and introduced into the mutant to obtain the comple…

CyclopropanesPhysiologyMembrane lipidsMutantApplied Microbiology and BiotechnologyGas Chromatography-Mass SpectrometryMembrane LipidsStress PhysiologicalMembrane fluidityViability assayPhospholipidsUnsaturated fatty acidMicrobial ViabilityEcologybiologyLactococcus lactis subsp cremorisFatty AcidsGenetic Complementation TestLactococcus lactisMethyltransferasesbiology.organism_classificationLactococcus lactisBiochemistryFatty Acids UnsaturatedMutant ProteinsAcidsBacteriaFood ScienceBiotechnologyApplied and Environmental Microbiology
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Engineering of a bacterial tyrosinase for improved catalytic efficiency towards D-tyrosine using random and site directed mutagenesis approaches

2013

The tyrosinase gene from Ralstonia solanacearum (GenBank NP518458) was subjected to random mutagenesis resulting in tyrosinase variants (RVC10 and RV145) with up to 3.2-fold improvement in kcat, 5.2-fold lower Km and 16-fold improvement in catalytic efficiency for D-tyrosine. Based on RVC10 and RV145 mutated sequences, single mutation variants were generated with all variants showing increased kcat for D-tyrosine compared to the wild type (WT). All single mutation variants based on RV145 had a higher kcat and Km value compared to the RV145 and thus the combination of four mutations in RV145 was antagonistic for turnover, but synergistic for affinity of the enzyme for D-tyrosine. Single muta…

DNA BacterialProtein ConformationSequence analysisTyrosinasehomology modelingMolecular Sequence DataMutation Missenserandom mutagenesisBioengineeringtyrosinaseProtein Engineering010402 general chemistry01 natural sciencesApplied Microbiology and Biotechnologyenzyme catalysis03 medical and health sciencessite specific mutagenesisMissense mutationSite-directed mutagenesisHistidine030304 developmental biology0303 health sciencesRalstonia solanacearumbiologyMonophenol MonooxygenaseWild typeActive siteSequence Analysis DNAbiology.organism_classificationMolecular biologyRecombinant Proteins0104 chemical sciencesKineticsMutagenesisRalstonia solanacearumbiology.proteinTyrosineD-tyrosineMutant ProteinsBiotechnology
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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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Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

2012

Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoprotein…

Halobacterium salinarumModels MolecularProtein FoldingProtein Denaturation01 natural sciencesBiotecnologiaBiochemistryBiophysics Simulationschemistry.chemical_compoundSensory RhodopsinsHalobacterium salinarum0303 health sciencesMultidisciplinarybiologyProtein StabilityQRTemperatureUltraviolet-visible spectroscopyThermal stabilityBacterial BiochemistryChemistryBiochemistryBacteriorhodopsinsRetinaldehydeMedicineProtonsResearch ArticleSteric effectsHydrogen bondingBioquímicaProtein StructureScienceRetinal bindingBiophysics010402 general chemistryMicrobiologyPhosphates03 medical and health sciencesBiology030304 developmental biologyAspartic AcidBinding SitesAdaptation OcularOrganic ChemistryOrganic SynthesisProteinsChromoproteinsRetinalBacteriorhodopsinBacteriologyBiological TransportChromophorebiology.organism_classification0104 chemical sciencesTransmembrane ProteinschemistryRetinaldehydeBiophysicsbiology.proteinMutant ProteinsPLoS ONE
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Respiratory behaviour of a Zymomonas mobilis adhB::kan(r) mutant supports the hypothesis of two alcohol dehydrogenase isoenzymes catalysing opposite …

2006

AbstractPerturbation of the aerobic steady-state in a chemostat culture of the ethanol-producing bacterium Zymomonas mobilis with a small pulse of ethanol causes a burst of ethanol oxidation, although the reactant ratio of the alcohol dehydrogenase (ADH) reaction ([NADH][acetaldehyde][H+])/([ethanol][NAD+]) remains above the Keq value. Simultaneous catalysis of ethanol synthesis and oxidation by the two ADH isoenzymes, residing in different redox microenvironments, has been proposed previously. In the present study, this hypothesis is verified by construction of an ADH-deficient strain and by demonstration that it lacks the oxidative burst in response to perturbation of its aerobic steady-s…

Kanamycin ResistanceBiophysicsMetabolic channellingChemostatBiochemistryRedoxZymomonas mobilisModels BiologicalCatalysischemistry.chemical_compoundContinuous cultureStructural BiologyGeneticsEthanol metabolismMolecular BiologyAlcohol dehydrogenaseZymomonasEthanolbiologyEthanolChemistryRespirationZymomonas mobilisAcetaldehydeAlcohol DehydrogenaseCell Biologybiology.organism_classificationAerobiosisIsoenzymesKineticsBiochemistrybiology.proteinMutant ProteinsNAD+ kinaseFEBS letters
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ALDH1A3 Mutations Cause Recessive Anophthalmia and Microphthalmia

2013

Anophthalmia and microphthalmia (A/M) are early-eye-development anomalies resulting in absent or small ocular globes, respectively. A/M anomalies occur in syndromic or nonsyndromic forms. They are genetically heterogeneous, some mutations in some genes being responsible for both anophthalmia and microphthalmia. Using a combination of homozygosity mapping, exome sequencing, and Sanger sequencing, we identified homozygosity for one splice-site and two missense mutations in the gene encoding the A3 isoform of the aldehyde dehydrogenase 1 (ALDH1A3) in three consanguineous families segregating A/M with occasional orbital cystic, neurological, and cardiac anomalies. ALDH1A3 is a key enzyme in the…

MaleGenetic LinkageRetinoic acidGenes RecessiveBiologymedicine.disease_causeMicrophthalmiachemistry.chemical_compoundsymbols.namesakeChromosome SegregationReportmedicineGeneticsFood and NutritionHumansMicrophthalmosMissense mutationGenetics(clinical)Genetics (clinical)Exome sequencingSanger sequencingGeneticsMutationAnophthalmiaHomozygoteAnophthalmosExonsSequence Analysis DNAAldehyde DehydrogenaseDisease gene identificationmedicine.diseaseAldehyde OxidoreductasesMolecular biologyIntronseye diseasesPedigreeHEK293 CellschemistryAlimentation et NutritionMutationsymbolsFemaleMutant Proteinssense organsThe American Journal of Human Genetics
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