Search results for "amino acid sequence"

showing 10 items of 1296 documents

Characterisation of a Cryptosporidium parvum-specific cDNA clone and detection of parasite DNA in mucosal scrapings of infected mice.

1998

A cDNA library was constructed using total RNA extracted from oocysts and sporozoites of the protozoan parasite Cryptosporidium parvum. The expression library was screened with an anti-C. parvum antiserum and a clone, Cp3.4, with a 2043 bp insert, was extracted. Southern blot analysis demonstrated a single copy gene that was located on a 1.6 Mb chromosome. The gene was found to be C. parvum specific as Cp3.4 did not cross-hybridise with chromosomal DNA from three other apicomplexan parasites. The cDNA encodes a polypeptide with a predicted membrane helix at its C-terminal end which is flanked by stretches of acidic amino acids. Overall, the polypeptide has a low isoelectric point (pI) of 3.…

DNA ComplementaryGenes ProtozoanMolecular Sequence DataProtozoan ProteinsCryptosporidiosisBiologyMolecular cloninglaw.inventionMicelawIleumComplementary DNAparasitic diseasesParasite hostingAnimalsAmino Acid SequenceRNA MessengerCloning MolecularIntestinal MucosaMolecular BiologyGenePolymerase chain reactionSouthern blotRepetitive Sequences Nucleic AcidCryptosporidium parvumcDNA libraryReverse Transcriptase Polymerase Chain ReactionChromosome MappingSequence Analysis DNADNA Protozoanbiology.organism_classificationMolecular biologyElectrophoresis Gel Pulsed-FieldBlotting SouthernCryptosporidium parvumParasitologyRNA ProtozoanMolecular and biochemical parasitology
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Cloning and tissue expression of two cDNAs encoding the peroxisomal 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea pig liver

1996

Abstract The 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD) is the second enzyme of the peroxisomal β-oxidation pathway. In human and rat, only one HD mRNA has been so far detected in the liver. This paper reports for the first time in a mammal species, the guinea pig, the cloning and sequencing of two cDNAs encoding an HD. The 3,274 nucleotide-cDNA is a strictly identical but longer copy of the 2,494 nucleotide-form. A 2,178 by-open reading frame encodes a protein of 726 amino acids ( M r 79.3 kDa) with the peroxisomal-targeting signal (tripeptide SKL) at the carboxyterminus. Northern blot analysis of HD mRNA identified three mRNAs of respective sizes 3.5, 2.6 and 1.6 kb in the…

DNA ComplementaryGuinea PigsMolecular Sequence DataBiophysicsGene ExpressionDehydrogenasePeroxisomeBiologyKidneyMicrobodiesBiochemistryStructural BiologyComplementary DNAGeneticsAnimalsPhosphofructokinase 2Amino Acid SequenceRNA MessengerNorthern blotCloning Molecular2-Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseBifunctional enzymeEnoyl-CoA HydrataseMolecular BiologyCloningBase Sequence3-Hydroxyacyl CoA DehydrogenasesSequence Analysis DNACell BiologyPeroxisomeEnoyl-CoA hydrataseBlotting NorthernGuinea pigMolecular biology3-Hydroxyacyl-CoA DehydrogenaseLiverBiochemistrycDNAFEBS Letters
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Isolation of Mhc class I cDNAs from the axolotl Ambystoma mexicanum.

1997

Class I major histocompatibility complex (Mhc) cDNA clones were isolated from axolotl mRNA by polymerase chain reaction (PCR) and by screening a cDNA phage library. The nucleotide and predicted amino acid sequences show definite similarities to the Mhc class Ialpha molecules of higher vertebrates. Most of the amino acids in the peptide binding region that dock peptides at their N and C termini in mammals are conserved. Several amino acids considered to be important for the interaction of beta2-microglobulin with the Mhc alpha chain are also conserved in the axolotl sequence. The fact that axolotl class I A cDNAs are ubiquitously expressed and highly polymorphic in the alpha1 and alpha2 doma…

DNA ComplementaryImmunologyMolecular Sequence DataGene ExpressionGenes MHC Class IPeptide bindingMajor histocompatibility complexAxolotlComplementary DNASequence Homology Nucleic AcidMHC class IGeneticsAnimalsTissue DistributionAmino Acid SequenceCloning MolecularAmbystoma mexicanumGenechemistry.chemical_classificationGeneticsBinding SitesPolymorphism GeneticbiologyBase SequenceSequence Homology Amino Acidbiology.organism_classificationAmino acidProtein Structure TertiaryAmbystoma mexicanumchemistrybiology.proteinSequence AlignmentImmunogenetics
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A frame shift mutation in a hot spot region of the nuclear autoantigen La (SS-B).

1996

A hot spot region was identified in the exon 7 of the nuclear autoantigen La (SS-B). Two La cDNAs were identified which contained a frame shift mutation in the hot spot region. One La cDNA was isolated from a cDNA library made from peripheral blood lymphocytes of an autoimmune patient with primary Sjogren's Syndrome, the other La cDNA was isolated from a human liver cDNA library. The patient's La cDNA had a deletion and the liver La cDNA had an insert of an (A)-residue at the same position. Inserts of 4, 16 and 24 more or less homogeneous (A)-residues were found at the same site in the three La retropseudogenes. The hot spot region located in one of the major autoepitope regions of the La a…

DNA ComplementaryImmunologyMolecular Sequence DataRNA-dependent RNA polymeraseBiologyTransfectionAutoantigensFrameshift mutationExonMiceComplementary DNAImmunology and AllergyAnimalsHumansAmino Acid SequenceRNA MessengerFrameshift MutationPeptide sequenceDNA PrimersMessenger RNABase SequencecDNA library3T3 CellsExonsVirologyMolecular biologyStop codonSjogren's SyndromeRibonucleoproteinsPseudogenesJournal of autoimmunity
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Diversity of stonefly hexamerins and implication for the evolution of insect storage proteins

2007

Hexamerins are large storage proteins of insects in the 500 kDa range that evolved from the copper-containing hemocyanins. Hexamerins have been found at high concentration in the hemolymph of many insect taxa, but have remained unstudied in relatively basal taxa. To obtain more detailed insight about early hexamerin evolution, we have studied hexamerins in stoneflies (Plecoptera). Stoneflies are also the only insects for which a functional hemocyanin is known to co-occur with hexamerins in the hemolymph. Here, we identified hexamerins in five plecopteran species and obtained partial cDNA sequences from Perla marginata (Perlidae), Nemoura sp. (Nemouridae), Taeniopteryx burksi (Taeniopterygid…

DNA ComplementaryInsectaMolecular Sequence DataZoologyPerlidaeBiochemistryEvolution MolecularSequence Analysis ProteinPhylogeneticsBotanyHemolymphAnimalsCapniidaeAmino Acid SequenceCloning MolecularMolecular clockMolecular BiologyPhylogenyTaeniopterygidaebiologyPhylogenetic treeSequence Analysis DNANemouridaebiology.organism_classificationInsect ScienceInsect ProteinsSequence AlignmentInsect Biochemistry and Molecular Biology
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Molecular characterization of hemocyanin and hexamerin from the firebrat Thermobia domestica (Zygentoma).

2008

Hexapods possess a tracheal system that enables the transport of oxygen to the inner organs. Although respiratory proteins have been considered unnecessary in most Hexapoda for this reason, we recently showed the presence of a functional hemocyanin in the stonefly Perla marginata. Here we report the identification and molecular characterization of a hemocyanin from Zygentoma (Thysanura). We obtained the full length cDNA of two distinct subunit types from the firebrat Thermobia domestica, and partial sequences of the orthologs from the silverfish Lepisma saccharina. The native T. domestica hemocyanin subunits both consist of 658 amino acids, but a signal peptide for transmembrane transport i…

DNA ComplementaryInsectaProtein subunitmedicine.medical_treatmentMolecular Sequence DataBiochemistrychemistry.chemical_compoundSequence Analysis ProteinHemolymphHemolymphAromatic amino acidsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyPhylogenybiologyHemocyaninbiology.organism_classificationThysanuraProtein SubunitschemistryBiochemistryInsect ScienceHemocyaninsInsect ProteinsThermobiaPterygota (plant)FirebratSequence AlignmentInsect biochemistry and molecular biology
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A respiratory hemocyanin from an insect.

2004

Insects possess an elaborate tracheal system that enables transport of gaseous oxygen from the atmosphere directly to the inner organs. Therefore, the presence of specialized oxygen-transport proteins in the circulatory system of insects has been considered generally unnecessary. Here, we show for the first time, to our knowledge, the presence of an ancestral and functional hemocyanin (Hc) in an insect. In the hemolymph of nymphs and adults of the stonefly Perla marginata , a hexameric Hc was identified, which consists of two distinct subunit types of 659 and 655 amino acids. P. marginata Hc displays cooperative oxygen binding with a moderately high oxygen affinity [(half-saturation pressu…

DNA ComplementaryInsectamedicine.medical_treatmentProtein subunitmedia_common.quotation_subjectMolecular Sequence DataInsectBiologyEvolution MolecularCrustaceaHemolymphHemolymphmedicineAnimalsAmino Acid SequenceCloning MolecularNymphPhylogenymedia_commonchemistry.chemical_classificationMultidisciplinaryBase SequenceSequence Homology Amino AcidRespirationHemocyaninBiological SciencesAmino acidRespiratory proteinOxygenProtein SubunitschemistryBiochemistryHemocyaninsInsect ProteinsFemaleOxygen bindingProceedings of the National Academy of Sciences of the United States of America
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Molecular cloning and expression of Tenebrio molitor ultraspiracle during metamorphosis and in vivo induction of its phosphorylation by 20-hydroxyecd…

2000

Using a RT-PCR approach, the Tenebrio molitor homologue of Drosophila Ultraspiracle (TmUSP) was characterized. Its DNA binding domain shows a degree of identity with those of the other insect USPs. However, the ligand binding domain is closer to those of retinoid X receptors. Using an antibody raised against DmUSP, Western blot analysis of proteins from epidermis and other tissues revealed five immunoreactive bands, corresponding to different phosphorylated forms of a unique polypeptide, as shown by lambda-phosphatase treatment. The nuclear form of TmUSP seems unphosphorylated. An in vivo 20-hydroxyecdysone treatment increases considerably and rapidly the phosphorylated forms of TmUSP. This…

DNA ComplementaryMolecular Sequence Data20-HydroxyecdysoneGene ExpressionMolecular cloningBiologychemistry.chemical_compoundWestern blotGene expressionGeneticsmedicineAnimalsDrosophila ProteinsHumansProtein IsoformsAmino Acid SequenceRNA MessengerCloning MolecularPhosphorylationReceptorTenebrioMolecular BiologyEpidermis (botany)medicine.diagnostic_testMetamorphosis BiologicalDNA-binding domainSequence Analysis DNAMolecular biologyCell biologyDNA-Binding ProteinsEcdysteronechemistryInsect SciencePhosphorylationEpidermisTranscription FactorsInsect molecular biology
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Analysis of expression of an alternative La (SS-B) cDNA and localization of the encoded N- and C-terminal peptides

1997

AbstractA deletion of an (A)-residue was detected in a cDNA encoding for the nuclear autoantigen La/SS-B. The cDNA was recently isolated from a cDNA library made from peripheral blood lymphocytes of a patient with primary Sjögren's Syndrome. The region, where the deletion occurred, represents a hot spot region in the La gene(s). It leads to a frame shift mutation and a premature stop codon eleven amino acids downstream of the deletion site within one of the protease sensitive regions of the La protein. In spite of the frame shift mutation expression of full length La protein occurred efficiently in E. coli. Full length La protein was also made in SF9 cells infected with recombinant baculovi…

DNA ComplementaryMolecular Sequence DataBiologyAutoantigensCell LineFrameshift mutationSingle-stranded binding proteinComplementary DNAEscherichia coliConsensus sequenceProtein biosynthesisHumansAmino Acid SequenceGeneMolecular BiologyBase SequencecDNA libraryCell BiologyMolecular biologyPeptide FragmentsSjogren's SyndromeRibonucleoproteinsCytoplasmMutationbiology.proteinBaculoviridaeGene DeletionBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Isolation and cloning of a C-type lectin from the hexactinellid sponge Aphrocallistes vastus: a putative aggregation factor

2001

Among the sponges (Porifera), the oldest group of metazoans in phylogenetic terms, the Hexactinellida is considered to have diverged earliest from the two other sponge classes, the Demospongiae and Calcarea. The Hexactinellida are unusual among all Metazoa in possessing mostly syncytial rather than cellular tissues. Here we describe the purification of a cell adhesion molecule with a size of 34 kDa (in its native form; 24 kDa after deglycosylation) from the hexactinellid sponge Aphrocallistes vastus. This adhesion molecule was previously found to agglutinate preserved cells and membranes in a non-species-specific manner (Müller, W. E. G., Zahn, R. K, Conrad, J., Kurelec, B., and Uhlenbruck,…

DNA ComplementaryMolecular Sequence DataBiologyBiochemistryMicrobiologyCell membraneC-type lectinLectinsmedicineAnimalsLectins C-TypeAmino Acid SequenceCloning MolecularPeptide sequencePhylogenyDNA Primerschemistry.chemical_classificationBase SequenceSequence Homology Amino AcidCell adhesion moleculeLectinbiology.organism_classificationPoriferaAmino acidSpongemedicine.anatomical_structurechemistryBiochemistrybiology.proteinGlycoproteinGlycobiology
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