Search results for " Complementary"

showing 10 items of 280 documents

Sequence of the M28 dsRNA: Preprotoxin Is Processed to an α/β Heterodimeric Protein Toxin

1995

The killer and immunity phenotypes of K28 killer strains of Saccharomyces cerevisiae are determined by the 1.75-kb M28 dsRNA virus. In the plus strand, M28p, the K28 preprotoxin gene, comprises bases 13-1047 and is followed, after an additional 85 bases, by a 63-bp poly(A) sequence and a 553-base 3'-sequence. This 3'-sequence contains two potential stem-loop structures predicted to bind the L-A encoded cap-pol protein, initiating encapsidation; high-level expression results in curing of M1 dsRNA. Expression of M28p confers the complete K28 killer and immunity phenotype on a cell lacking M28 dsRNA. K28 toxin is a disulfide-bonded heterodimer of alpha (10.5 kDa) and beta (11 kDa) components w…

Signal peptideDNA ComplementaryGlycosylationSaccharomyces cerevisiae ProteinsGlycosylationMolecular Sequence DataMutantCarboxypeptidasesSaccharomyces cerevisiaeBiologymedicine.disease_causeCleavage (embryo)Fungal Proteinschemistry.chemical_compoundGene Expression Regulation FungalVirologyEndopeptidasesmedicineSecretionAmino Acid SequenceSubtilisinsGeneDNA PrimersRNA Double-StrandedBase SequenceToxinSerine EndopeptidasesMembrane ProteinsRNA FungalMycotoxinsMolecular biologyKiller Factors YeastRNA silencingchemistryProprotein ConvertasesProtein Processing Post-TranslationalVirology
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Structure, organization and expression of two clustered cuticle protein genes during the metamorphosis of an insect, Tenebrio molitor.

1998

A 4-kb DNA segment of Tenebrio molitor (Insecta, Coleoptera) genomic DNA containing two larval-pupal cuticular genes has been cloned and sequenced. These genes, transcribed in opposite directions, are related in DNA sequence and the proteins encoded are very similar. Each of them contains a single intron located inside the sequence encoding the signal peptide, and a conserved sequence at -200 bp from the mRNA start position. These similarities in sequence suggest that these genes have evolved by duplication followed by diversification and that they are members of a family of genes with a common ancestry. They are the first example of clustered genes in Tenebrio molitor.

Signal peptideDNA ComplementaryMolecular Sequence DataGenes InsectBiologyBiochemistryDNA sequencingConserved sequenceEvolution MolecularGene duplicationAnimalsAmino Acid SequenceTenebrioPeptide sequenceGeneIn Situ HybridizationGeneticsBase SequenceSequence Homology Amino AcidfungiIntronMetamorphosis BiologicalGene Expression Regulation DevelopmentalIntronsgenomic DNAMultigene FamilyInsect ProteinsEuropean journal of biochemistry
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Molecular cloning and primary structure of a Rhesus (Rh)-like protein from the marine sponge Geodia cydonium

1997

In humans, the 30,000 M(r) Rhesus (Rh) polypeptide D (RhD) is a dominant antigen (Ag) of the Rh blood group system. To date, an Rh-like protein has been found in chimpanzees, gorillas, gibbons, and rhesus monkeys. Related to the 30,000 M(r) Rh Ag protein are two polypeptides of 50,000 M(r), the human 50,000 M(r) Rh Ag and the RhD-like protein from Caenorhabditis elegans. The function of all these proteins is not sufficiently known. Here we characterize a cDNA clone (GCRH) encoding a putative 57,000 M(r) polypeptide from the marine sponge Geodia cydonium, which shares sequence similarity both to the RhD Ag and the Rh50 glycoprotein. The sponge Rh-like protein comprises 523 aa residues; hydro…

Signal peptideDNA ComplementaryMolecular Sequence DataImmunologyMolecular cloningGeneticsAnimalsHumansAmino Acid SequenceCloning MolecularCaenorhabditis elegansGlycoproteinschemistry.chemical_classificationRh-Hr Blood-Group SystemBase SequenceSequence Homology Amino AcidbiologyProtein primary structurebiology.organism_classificationMolecular biologyPoriferaSpongeTransmembrane domainchemistryGlycoproteinRh blood group systemImmunogenetics
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Complete sequence, expression and evolution of two members of the hexamerin protein family during the larval development of the rice moth, Corcyra ce…

2002

Three distinct types of storage hexamerins are expressed in the "last-instar" larvae of the rice moth, Corcyra cephalonica. A cDNA expression library was constructed from fat body-RNA and screened with a polyclonal antibody raised against purified hexamerin (SP2) of Corcyra cephalonica. Two slightly different "full-length" hexamerin cDNA clones (Hex2a and Hex2b) were isolated and sequenced. Both include open reading frames of 2109 bp which are translated into polypeptides of 703 amino acids with 92.5% identity. Signal peptides of 19 amino acids are present at the N-termini. The 684 amino acids native proteins have a high content of aryl groups (17.6%). According to both the criteria for ami…

Signal peptideDNA ComplementaryProtein familyBlotting WesternMolecular Sequence DataMothsBiochemistryEvolution MolecularComplete sequenceComplementary DNAEscherichia coliAnimalsAmino Acid SequenceMolecular BiologyGenePhylogenychemistry.chemical_classificationBase SequenceSequence Homology Amino AcidbiologyfungiBlotting Northernbiology.organism_classificationRecombinant ProteinsAmino acidOpen reading framechemistryBiochemistryRice mothLarvaInsect ScienceInsect ProteinsInsect Biochemistry and Molecular Biology
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mp23, a Theileria parva transmembrane protein with homology to the protein disulfide isomerase family

2002

The protozoan parasite Theileria parva (Apicomplexa) causes the bovine disease East Coast Fever in endemic areas in Subsaharan Africa. The intralymphocytic schizont stage is largely responsible for the pathogenicity and induces a transformed phenotype in host cells [1]. Current evidence supports a model in which the schizont perturbs the immune response by inducing production of cytokines and stimulating the growth of parasitized cells [2]. We were interested to identify parasite proteins involved in parasite/host interaction and have described earlier a screening procedure for identification of schizont stage-exported proteins based on cell-free expression of cDNA and testing for transloca…

Signal peptideDNA ComplementarySequence Homology Amino AcidcDNA libraryEndoplasmic reticulumTheileria parvaMolecular Sequence DataProtein Disulfide-IsomerasesProtozoan ProteinsMembrane ProteinsSequence Analysis DNABiologyTheileria parvabiology.organism_classificationMolecular biologyTransmembrane proteinMembrane proteinComplementary DNAparasitic diseasesAnimalsParasitologyAmino Acid SequenceProtein disulfide-isomeraseMolecular BiologyMolecular and Biochemical Parasitology
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A novel cell wall protein specific to the mycelial form of Yarrowia lipolytica.

1996

A cDNA clone specifying a cell wall protein was isolated from a Yarrowia lipolytica cDNA library. The cDNA library was constructed in the expression vector lambda gt 11, with the RNA isolated from actively growing mycelial cells. The deduced amino acid sequence shows that the encoded protein contains an N-terminal hydrophobic signal peptide. We have designated this protein YWP1 for Yarrowia lipolytica cell Wall Protein. Northern hybridization identified YWP1 transcript only when Y. lipolytica was growing in the mycelial form. The encoded protein seems to be covalently bound to the glucan cell wall since it is not released from the cell walls by sodium dodecyl sulphate extraction, but it is …

Signal peptideDNA ComplementaryTranscription GeneticHydrolasesBlotting WesternGenetic VectorsMolecular Sequence DataRestriction MappingBioengineeringApplied Microbiology and BiotechnologyBiochemistryCell wallFungal ProteinsOpen Reading FramesTransformation GeneticCell WallComplementary DNAGene Expression Regulation FungalYeastsGeneticsEscherichia coliAmino Acid SequenceCloning MolecularFluorescent Antibody Technique IndirectPeptide sequenceAntibodies FungalGene LibraryExpression vectorbiologyBase SequencecDNA libraryRNASodium Dodecyl SulfateYarrowiaRNA Fungalbiology.organism_classificationBlotting NorthernBlotting SouthernBiochemistrySaccharomycetalesElectrophoresis Polyacrylamide GelBiotechnologyYeast (Chichester, England)
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Diplopod hemocyanin sequence and the phylogenetic position of the Myriapoda

2001

Hemocyanins are copper-containing respiratory proteins of the Arthropoda that have so far been thoroughly investigated only in the Chelicerata and the Crustacea but have remained unstudied until now in the Myriapoda. Here we report the first sequence of a myriapod hemocyanin. The hemocyanin of Spirostreptus sp. (Diplopoda: Spirostreptidae) is composed of two distinct subunits that are arranged in a 6 x 6 native molecule. The cloned hemocyanin subunit cDNA codes of for a polypeptide of 653 amino acids (75.5 kDa) that includes a signal peptide of 18 amino acids. The sequence closely resembles that of the chelicerate hemocyanins. Molecular phylogenetic analyses reject with high statistical con…

Signal peptideDNA Complementarymedicine.medical_treatmentMolecular Sequence DataMyriapodachemical and pharmacologic phenomenaBiologycomplex mixturesEvolution MolecularSequence Analysis ProteinGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyArthropodsEcology Evolution Behavior and SystematicsPhylogenyPhylogenetic treeSequence Homology Amino Acidhemic and immune systemsHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationSpirostreptusSister groupEvolutionary biologyHemocyaninsChelicerataSequence AlignmentSpirostreptidae
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Isolation and characterization of two T-box genes from sponges, the phylogenetically oldest metazoan taxon

2003

It is now well established that all metazoan phyla derived from one common ancestor, the hypothetical Urmetazoa. Due to the basal position of Porifera (Demospongiae) in the phylogenetic tree of Metazoa, studies on the mechanisms controlling the development of these animals can provide clues on the understanding of the origin of multicellular animals and on how the first organization of the body plan evolved. In this report we describe the isolation and genomic characterization of two T-box genes from the siliceous sponge Suberites domuncula. The phylogenetic analysis classifies one into the subfamily of Brachyury, Sd-Bra, and the second into the Tbx2 subfamily, Sd-Tbx2. Analyses of the Sd-B…

Siliceous spongeBrachyuryDNA ComplementarySubfamilyMolecular Sequence DataMolecular evolutionPhylogeneticsGeneticsAnimalsProtein IsoformsElectrophoresis Gel Two-DimensionalAmino Acid SequencePhylogenyBase SequencebiologyPhylogenetic treeSequence Analysis DNAAnatomybiology.organism_classificationPoriferaSuberites domunculaAlternative SplicingBody planEvolutionary biologyT-Box Domain ProteinsProtein Processing Post-TranslationalDevelopmental BiologyDevelopment Genes and Evolution
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Engineering of chicken avidin: a progressive series of reduced charge mutants.

1998

Avidin, a positively charged egg-white glycoprotein, is a widely used tool in biotechnological applications because of its ability to bind biotin strongly. The high pI of avidin (approximately 10.5), however, is a hindrance in certain applications due to non-specific (charge-related) binding. Here we report a construction of a series of avidin charge mutants with pIs ranging from 9.4 to 4.7. Rational design of the avidin mutants was based on known crystallographic data together with comparative sequence alignment of avidin, streptavidin and a set of avidin-related genes which occur in the chicken genome. All charge mutants retained the ability to bind biotin tightly according to optical bio…

StreptavidinDNA ComplementaryHot TemperatureMutantBiophysicsBiotinSequence alignmentBiologySpodopteraProtein EngineeringBiochemistrychemistry.chemical_compoundstomatognathic systemBiotinStructural BiologyGeneticsAnimalsMolecular BiologyCharge mutantAvidin-biotin technologyRational designCell BiologyProtein engineeringrespiratory systemAvidinDNA-Binding ProteinschemistryBiochemistryBiotinylationbiology.proteinMutagenesis Site-DirectedChickensAvidinFEBS letters
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A G468-T AMPD1 mutant allele contributes to the high incidence of myoadenylate deaminase deficiency in the Caucasian population.

2002

Myoadenylate deaminase deficiency is the most common metabolic disorder of skeletal muscle in the Caucasian population, affecting approximately 2% of all individuals. Although most deficient subjects are asymptomatic, some suffer from exercise-induced myalgia suggesting a causal relationship between a lack of enzyme activity and muscle function. In addition, carriers of this derangement in purine nucleotide catabolism may have an adaptive advantage related to clinical outcome in heart disease. The molecular basis of myoadenylate deaminase deficiency in Caucasians has been attributed to a single mutant allele characterized by double C to T transitions at nucleotides +34 and +143 in mRNA enco…

ThreonineDNA ComplementaryGenotypeBlotting WesternGlycineMetabolic myopathyBiologyCompound heterozygosityPolymerase Chain ReactionWhite PeopleAMP DeaminaseMetabolic DiseasesMuscular DiseasesGenotypemedicineHumansAlleleTransversionMuscle SkeletalGenetics (clinical)AllelesElectromyographyPoint mutationMetabolic disorderAMP deaminasemedicine.diseaseMolecular biologyPhenotypeNeurologyPediatrics Perinatology and Child HealthMutationNeurology (clinical)DNA ProbesNeuromuscular disorders : NMD
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