Search results for " Site-Directed"

showing 10 items of 132 documents

Identification of a putative membrane-inserted segment in the alpha-toxin of Staphylococcus aureus.

1994

To gain a fuller understanding of the regions of the Staphylococcus aureus alpha-toxin important in pore formation, we have used Forster dipole-dipole energy transfer to demonstrate that a central glycine-rich region of alpha-toxin (the so-called "hinge" region) inserts deeply into the bilayer on association of toxin with liposomes. Mutant alpha-toxins with unique cysteine (C) residues at positions 69 and 130 [Palmer, M., et al. (1993) J. Biol. Chem. 268, 11959) were reacted with the C-specific fluorophore acrylodan, which acted as an energy donor. The chosen acceptor was N-(7-nitrobenz-2-oxa-13- diazol-4-yl)-1,2-bis(hexadecanoyl)-sn-glycero-3-phosphoethanolamin e (NBD-PE). Measurement of t…

LiposomeStaphylococcus aureusQuenching (fluorescence)FluorophoreStereochemistryBilayerPhosphatidylethanolaminesBacterial ToxinsLipid BilayersMembrane ProteinsFluorescence PolarizationBiochemistryAcceptorLipidschemistry.chemical_compoundHemolysin ProteinsMembranechemistryMutagenesis Site-DirectedStaphylococcus aureus delta toxinCysteineFluorescent DyesBiochemistry
researchProduct

Coupling of endothelin receptors to the ERK/MAP kinase pathway. Roles of palmitoylation and G(alpha)q.

2001

Endothelins are potent mitogens that stimulate extracellular signal-regulated kinases (ERK/MAP kinases) through their cognate G-protein-coupled receptors, ET(A) and ET(B). To address the role of post-translational ET receptor modifications such as acylation on ERK activation and to identify relevant downstream effectors coupling the ET receptor to the ERK signaling cascades we have constructed a panel of palmitoylation-deficient ET receptor mutants with differential G(alpha) protein binding capacity. Endothelin-1 stimulation of wild-type ET(A) or ET(B) induced a fivefold to sixfold increase in ERK in COS-7 and CHO cells whereas full-length nonpalmitoylated ET(A) and ET(B) mutants failed to …

MAPK/ERK pathwayGs alpha subunitInsectaMAP Kinase Signaling SystemBlotting WesternMolecular Sequence DataPalmitic AcidSRC Family Tyrosine KinaseBiochemistryCell LineCricetinaeArrestinTumor Cells CulturedAnimalsHumansAmino Acid SequenceReceptorMitogen-Activated Protein Kinase 1KinaseChemistryReceptors EndothelinCell MembraneHeterotrimeric GTP-Binding ProteinsCell biologyEnzyme ActivationErbB ReceptorsType C PhospholipasesCOS CellsMutationcardiovascular systemMutagenesis Site-DirectedPhosphorylationGTP-Binding Protein alpha Subunits Gq-G11Mitogen-Activated Protein KinasesProto-oncogene tyrosine-protein kinase SrcEuropean journal of biochemistry
researchProduct

p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
researchProduct

Synthesis and biological evaluation of cycloalkylidene carboxylic acids as novel effectors of Ras/Raf interaction.

2002

The protooncogenes Ras and Raf play important roles in signal transduction pathways regulated by mitogen-activated protein kinases. Mutations of Ras that arrest the protein in its active state are frequently implicated in tumor formation. We used Ras and Raf proteins in the yeast two-hybrid system to search for natural or synthesized substances capable of modulating Ras/Raf interaction by specifically binding to one of the interacting partners. We found that cycloalkylidene carboxylic acids enhanced Ras/Raf interaction by acting on the cysteine-rich domain of Raf. Several analogues of the active substance 2-cyclohexylidene propanoic acid were synthesized and the importance of the semicyclic…

MAPK/ERK pathwayMagnetic Resonance SpectroscopyCarboxylic acidSaccharomyces cerevisiaeAmino Acid MotifsCarboxylic AcidsAnti-apoptotic Ras signalling cascadeTwo-Hybrid System TechniquesDrug DiscoveryHumansHRASProtein kinase Achemistry.chemical_classificationbiologyChemistryKinasebiology.organism_classificationProtein Structure TertiaryProto-Oncogene Proteins c-rafBiochemistryModels ChemicalMutationMutagenesis Site-Directedras ProteinsMolecular MedicineSignal transductionPlasmidsProtein BindingJournal of medicinal chemistry
researchProduct

Genetics for Pseudoalteromonas provides tools to manipulate marine bacterial virus PM2

2008

ABSTRACT The genetic manipulation of marine double-stranded DNA (dsDNA) bacteriophage PM2 ( Corticoviridae ) has been limited so far. The isolation of an autonomously replicating DNA element of Pseudoalteromonas haloplanktis TAC125 and construction of a shuttle vector replicating in both Escherichia coli and Pseudoalteromonas enabled us to design a set of conjugative shuttle plasmids encoding tRNA suppressors for amber mutations. Using a host strain carrying a suppressor plasmid allows the introduction and analysis of nonsense mutations in PM2. Here, we describe the isolation and characterization of a suppressor-sensitive PM2 sus2 mutant deficient in the structural protein P10. To infect an…

MESH: Corticoviridae[SDV]Life Sciences [q-bio]Bacteriophages Transposons and PlasmidsMutantPlasmidPseudoalteromonasRNA TransferMESH: Genetic VectorsMESH: Models GeneticMESH: Capsid ProteinsGenetics0303 health sciencesbiologyMESH: Escherichia coliPseudoalteromonasMESH: Mutagenesis Site-DirectedPhenotypeMESH: DNA CircularElectrophoresis Polyacrylamide GelDNA CircularMESH: Genome ViralPlasmidsMESH: MutationGenetic VectorsGenome ViralMESH: PhenotypeMicrobiologyPseudoalteromonas haloplanktisViral Proteins03 medical and health sciencesShuttle vectorMESH: PlasmidsHost outer membraneEscherichia coliSeawaterMolecular Biology030304 developmental biologyModels Genetic030306 microbiologyMESH: PseudoalteromonasCorticoviridaeMESH: SeawaterViral membranebiology.organism_classificationMESH: RNA TransferMESH: Viral Proteins[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyMutationMutagenesis Site-DirectedCapsid ProteinsBacterial virusMESH: Electrophoresis Polyacrylamide Gel
researchProduct

The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase

2003

The mammalian soluble epoxide hydrolase (sEH) is an enzyme with multiple functions, being implicated in detoxification of xenobiotic epoxides as well as in regulation of physiological processes such as blood pressure. The enzyme is a homodimer, in which each subunit is composed of two domains. The 35-kDa C-terminal domain has an α/β hydrolase fold and harbors the catalytic center for the EH activity. The 25-kDa N-terminal domain has a different α/β fold and belongs to the haloacid dehalogenase superfamily of enzymes. The catalytic properties of the enzyme reported so far can all be explained by the action of the C-terminal domain alone. The function of the N-terminal domain, other than in …

MaleModels MolecularEpoxide hydrolase 2HydrolasesStereochemistryProtein subunitMolecular Sequence DataPhosphatase10050 Institute of Pharmacology and Toxicology610 Medicine & healthDephosphorylationHydrolaseAnimalsHumansAmino Acid SequenceDNA PrimersEpoxide Hydrolaseschemistry.chemical_classification1000 MultidisciplinaryMultidisciplinaryBase SequenceSequence Homology Amino AcidbiologyChemistryActive siteBiological SciencesPhosphoric Monoester HydrolasesRats Inbred F344Recombinant ProteinsRatsAmino acidEnzymeSolubilityBiochemistryMutagenesis Site-Directedbiology.protein570 Life sciences; biologyProceedings of the National Academy of Sciences
researchProduct

Construction of hevein (Hev b 6.02) with reduced allergenicity for immunotherapy of latex allergy by comutation of six amino acid residues on the con…

2004

Abstract Recently we have established that IgE Abs bind to conformational epitopes in the N- and C-terminal regions of the major natural rubber latex allergen, hevein (Hev b 6.02). To identify the critical amino acid residues that interact with IgE, the hevein sequence was scanned by using site-specific mutations. Twenty-nine hevein mutants were designed and produced by a baculovirus expression system in insect cells and tested by IgE inhibition-ELISA using sera from 26 latex allergic patients. Six potential IgE-interacting residues of hevein (Arg5, Lys10, Glu29, Tyr30, His35, and Gln38) were identified and characterized further in detail. Based on these six residues, two triple mutants (HΔ…

MaleModels MolecularProtein ConformationMutantImmunoglobulin Emedicine.disease_causeEpitopelaw.inventionEpitopes0302 clinical medicineProtein structureAllergenlawImmunology and AllergyCombinatorial Chemistry TechniquesChild0303 health sciencesbiologyChemistryMiddle AgedRecombinant Proteins3. Good healthBiochemistryLatex allergyRecombinant DNAFemalePlant LectinsProtein BindingAdultAdolescentImmunologyMutagenesis (molecular biology technique)Binding Competitive03 medical and health sciencesLatex HypersensitivitymedicineHumansPoint Mutation030304 developmental biologyAgedAllergensImmunoglobulin Emedicine.disease030228 respiratory systemAmino Acid SubstitutionDesensitization Immunologicbiology.proteinMutagenesis Site-DirectedBinding Sites AntibodyAntimicrobial Cationic PeptidesJournal of immunology (Baltimore, Md. : 1950)
researchProduct

Natural and engineered carboxy-terminal variants: decreased secretion and gain-of-function result in asymptomatic coagulation factor VII deficiency.

2012

We report 2 asymptomatic homozygotes for the nonsense p.R462X mutation affecting the carboxy-terminus of coagulation factor VII (FVII, 466 aminoacids). FVII levels of 3-5% and 2.7 ± 0.4% were found in prothrombin time-based and activated factor X (FXa) generation assays with human thromboplastins. Noticeably, FVII antigen levels were barely detectable (0.7 ± 0.2%) which suggested a gain-of-function effect. This effect was more pronounced with bovine thromboplastin (4.8 ± 0.9%) and disappeared with rabbit thromboplastin (0.7 ± 0.2%). This suggests that the mutation influences tissue factor/FVII interactions. Whereas the recombinant rFVII-462X variant confirmed an increase in specific activit…

MaleProteasesHeterozygoteFactor VII DeficiencyEnzyme-Linked Immunosorbent AssayFVIIBiologymedicine.disease_causeThromboplastinTissue factorchemistry.chemical_compoundCarboxy-terminalhemic and lymphatic diseasesmedicineFACTOR VII DEFICIENCY MOLECULAR VARIANTSThromboplastinMissense mutationAnimalsHumanscardiovascular diseasesChildBlood CoagulationProthrombin timeMutationmedicine.diagnostic_testFactor VIIHomozygoteHematologyFactor VIIMiddle AgedMolecular biologyAsymptomatic; Carboxy-terminal; FVII; Mutation;AsymptomaticchemistryCoagulationCodon NonsenseMutationMutagenesis Site-DirectedProthrombin TimeCattleFemaleRabbitsOriginal Articles and Brief Reports
researchProduct

Haploinsufficiency of ATP1A2 encoding the Na+/K+ pump alpha2 subunit associated with familial hemiplegic migraine type 2.

2003

Headache attacks and autonomic dysfunctions characterize migraine, a very common, disabling disorder with a prevalence of 12% in the general population of Western countries(1,2). About 20% of individuals affected with migraine experience aura, a visual or sensory-motor neurological dysfunction that usually precedes or accompanies the headache(3). Although the mode of transmission is controversial(4), population-based and twin studies have implicated genetic factors, especially in migraine with aura(5,6). Familial hemiplegic migraine is a hereditary form of migraine characterized by aura and some hemiparesis. Here we show that mutations in the gene ATP1A2 that encodes the alpha2 subunit of t…

Malemedicine.medical_specialtyAuraCell SurvivalPopulationMigraine with AuraMolecular Sequence DataDrug ResistanceBiologyHaploidyTransfectionATP1A2Internal medicineATP1A3Chlorocebus aethiopsGeneticsmedicineAnimalsHumansEnzyme InhibitorseducationOuabainFamilial hemiplegic migraineChromatography High Pressure LiquidGeneticseducation.field_of_studyBase Sequencemedicine.diseaseMigraine with auraPeptide FragmentsPedigreeEndocrinologyMigraineChromosomes Human Pair 1Case-Control StudiesCOS CellsMutationMutagenesis Site-DirectedFemaleCalcium Channelsmedicine.symptomSodium-Potassium-Exchanging ATPaseHaploinsufficiencyHeLa CellsNature genetics
researchProduct

The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6

2017

Studying folding and assembly of naturally occurring α-helical transmembrane proteins can inspire the design of membrane proteins with defined functions. Thus far, most studies have focused on the role of membrane-integrated protein regions. However, to fully understand folding pathways and stabilization of α–helical membrane proteins, it is vital to also include the role of soluble loops. We have analyzed the impact of interhelical loops on folding, assembly and stability of the heme-containing four-helix bundle transmembrane protein cytochrome b6 that is involved in charge transfer across biomembranes. Cytochrome b6 consists of two transmembrane helical hairpins that sandwich two heme mol…

Metabolic ProcessesProtein FoldingProtein StructureSurfactantsCell MembranesMaterials ScienceDetergentslcsh:MedicineHemeBiochemistrySpinacia oleraceaddc:570Macromolecular Structure AnalysisRNA stem-loop structure500 Natural sciences and mathematicsAmino Acid SequencePost-Translational ModificationEnzyme ChemistryRNA structurelcsh:ScienceMolecular BiologyMaterials by Attributelcsh:RMembrane ProteinsBiology and Life SciencesProteinsProteasesCell BiologyEnzymesNucleic acidsMetabolismCytochromes b6ProteolysisPhysical SciencesMutagenesis Site-DirectedEnzymologyCofactors (Biochemistry)RNAlcsh:Q500 NaturwissenschaftenCellular Structures and OrganellesDimerizationResearch Article
researchProduct