Search results for "Base Sequence"

showing 10 items of 1146 documents

Cloning of a cDNA fragment encoding part of the protein moiety of the 58-kDa fibrinogen-binding mannoprotein of Candida albicans

2006

Immunoscreening of a Candida albicans expression library with antibodies against the 58 kDa fibrinogen-binding mannoprotein (mp58) of the fungus resulted in the isolation of clones encoding the protein moiety of this molecule. Sequence of the 0.9 kb cDNA of one of the clones selected for further analysis, revealed an open reading frame coding for 292 amino acids, which displays sequence similarity to proteins belonging to a family of immunodominant antigens of Aspergillus spp. The gene corresponding to this cDNA was named FBP1 (fibrinogen-binding protein). These results represent the first report on the identification of C. albicans genes encoding surface receptors for host proteins.

DNA ComplementaryGenes FungalMolecular Sequence DataSequence alignmentMicrobiologyFungal ProteinsCell WallComplementary DNAImmunoscreeningCandida albicansCell AdhesionGeneticsAmino Acid SequenceCloning MolecularCandida albicansMolecular BiologyPeptide sequenceBase SequenceSequence Homology Amino AcidbiologyFibrinogenFibrinogen bindingbiology.organism_classificationMolecular biologyCorpus albicansMolecular WeightBlotting SouthernOpen reading frameCell Adhesion MoleculesSequence AlignmentFEMS Microbiology Letters
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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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A comparative analysis to study editing of small noncoding BC200- and Alu transcripts in brain of prion-inoculated rhesus monkeys (M. Mulatta).

2012

Small retroelements (short interspersed elements, abbreviated SINEs) are abundant in vertebrate genomes. Using RNA isolated from rhesus monkey cerebellum and buffy coat, reverse-transcription polymerase chain reaction (RT PCR) was applied to clone cDNA of BC200 and Alu RNAs. Transcripts containing Alu-SINE sequences may be subjected to extensive RNA editing by ADAR (adenosine deaminases that act on RNA) deamination. Abundance of Alu transcripts was determined with real-time RT PCR and was significantly higher than BC200 (brain cytoplasmic) in cerebellum. BC200 transcripts were absent from buffy coat cells. Availability of the rhesus genome sequence allowed the BC200 transcripts to be mapped…

DNA ComplementaryHealth Toxicology and MutagenesisMolecular Sequence DataRNA-dependent RNA polymeraseBiologyToxicologyReal-Time Polymerase Chain ReactionRNA polymerase IIICreutzfeldt-Jakob SyndromeAlu ElementsComplementary DNACerebellumAnimalsShort Interspersed Nucleotide ElementsGeneticsBase SequenceReverse Transcriptase Polymerase Chain ReactionIntronRNARNA Polymerase IIISequence Analysis DNAMolecular biologyMacaca mulattaReal-time polymerase chain reactionRNA editingADARRNARNA Small UntranslatedRNA EditingJournal of toxicology and environmental health. Part A
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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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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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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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An insect juvenile hormone-specific epoxide hydrolase is related to vertebrate microsomal epoxide hydrolases.

1996

Abstract We describe the first cDNA sequence encoding a juvenile hormone-specific epoxide hydrolase from an insect. A full-length cDNA clone revealed a 462-amino-acid open reading frame encoding an amino acid sequence with 44% identity and 64% similarity to human microsomal epoxide hydrolase. All residues in the catalytic triad (residues Asp 227 -His 428 -Asp 350 in the M. sexta protein) were present, as was the conserved Trp 154 corresponding to the oxyanion hole. The surprising similarity of insect juvenile hormone epoxide hydrolase to vertebrate microsomal epoxide hydrolases, coupled with the ancient lineage of the epoxide hydrolases and haloalkane dehalogenases, suggests that this catab…

DNA ComplementaryMolecular Sequence DataBiophysicsSequence HomologyBiologyBiochemistryPolymerase Chain ReactionMiceOpen Reading FramesComplementary DNAMicrosomesCatalytic triadAnimalsHumansAmino Acid SequenceEpoxide hydrolaseMolecular BiologyPeptide sequenceConserved SequenceEpoxide HydrolasesBase SequenceCell BiologyRatsJuvenile HormonesBiochemistryMicrosomal epoxide hydrolaseEpoxide HydrolasesJuvenile hormoneRabbitsOxyanion holeBiochemical and biophysical research communications
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Cloning and sequencing of the cDNA encoding human glutaredoxin.

1994

Glutaredoxin (thioltransferase) is a small, heat-stable protein, which is involved in thiol/disulfide exchange reactions. We have isolated a cDNA that encodes glutaredoxin from a human brain cDNA library. The encoded protein contains 106 amino acids with a calculated molecular mass of 11.76 kDa and an isoelectric point of 8.09. The amino acid sequence deduced from the cDNA is more than 80% identical to those of other mammalian glutaredoxins.

DNA ComplementaryMolecular Sequence DataBiophysicsSequence alignmentMolecular cloningBiologyBiochemistryStructural BiologyGlutaredoxinComplementary DNAGeneticsHumansAmino Acid SequenceCloning MolecularPeptide sequenceGlutaredoxinschemistry.chemical_classificationBase SequencecDNA libraryNucleic acid sequenceBrainProteinsMolecular biologyAmino acidchemistryBiochemistryOxidoreductasesBiochimica et biophysica acta
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