Search results for " Homology"

showing 10 items of 633 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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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 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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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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Neuroglobins from the Zebrafish Danio rerio and the Pufferfish Tetraodon nigroviridis

2001

Neuroglobin is a recently discovered respiratory, porphyrin-containing protein that is expressed in the brain of mouse and man. Here we show that neuroglobin is also present in the teleost fish. Complete cDNA sequences are reported from the pufferfish Tetraodon nigroviridis and the zebrafish Danio rerio. In addition, the neuroglobin gene of T. nigroviridis was sequenced, demonstrating the conservation of the B12.2, E11.0 and G7.0 introns plus the presence of an additional intron in the 5' noncoding region. The fish neuroglobins each comprise 159 amino acids and are 84.3% identical. Phylogenetic analyses show a basal position of the neuroglobins within the metazoan globin tree. An enhanced a…

DNA ComplementaryMolecular Sequence DataBiophysicsDanioNeuroglobinNerve Tissue ProteinsEyeTetraodon nigroviridisBiochemistryComplementary DNAAnimalsAmino Acid SequenceGlobinCloning MolecularMolecular BiologyZebrafishPhylogenyZebrafishchemistry.chemical_classificationGeneticsSequence Homology Amino AcidbiologyIntronCell Biologybiology.organism_classificationGlobinsAmino acidchemistryNeuroglobinBiochemical and Biophysical Research Communications
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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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A novel member of an ancient superfamily: sponge (Geodia cydonium, Porifera) putative protein that features scavenger receptor cysteine-rich repeats

1997

Proteins featuring scavenger receptor cysteine-rich (SRCR) domains are prominent receptors known from vertebrates and from one phylum of invertebrates, the echinoderms. In the present study we report the first putative SRCR protein from the marine sponge Geodia cydonium (Porifera), a member of the lowest phylum of contemporary Metazoans. Two forms of SRCR molecules were characterized, which apparently represent alternative splicing of the same transcript. The long putative SRCR protein, of 1536 aa, features twelve SRCR repeats, a C-terminal transmembrane domain and a cytoplasmic tail. The sequence of the short form is identical with the long form except that it lacks a coding region near th…

DNA ComplementaryMolecular Sequence DataCell-cell recognitionReceptors Cell SurfaceBiologyHomology (biology)PhylogeneticsSequence Homology Nucleic AcidGeneticsAnimalsCoding regionAmino Acid SequenceCysteineCloning MolecularReceptors ImmunologicScavenger receptorConserved SequenceReceptors LipoproteinRepetitive Sequences Nucleic AcidReceptors ScavengerGeneticsBase SequenceC-terminusAlternative splicingMembrane ProteinsGeneral MedicineScavenger Receptors Class BBiological EvolutionPoriferaTransmembrane domainGene
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Axial (apical-basal) expression of pro-apoptotic and pro-survival genes in the lake baikal demosponge Lubomirskia baicalensis.

2006

Like in all other Metazoa, also in sponges (Porifera) proliferation, differentiation, and death of cells are controlled by apoptotic processes, thus allowing the establishment of a Bauplan (body plan). The demosponge Lubomirskia baicalensis from the Lake Baikal is especially suitable to assess the role of the apoptotic molecules, since its grade of construction is highly elaborated into an encrusting base and branches composed of modules lined up along the apical-basal axis. The four cDNAs, ALG-2, BAK, MA-3, and Bcl-2, were isolated from this sponge species. The expression levels of these genes follow characteristic gradients. While the proapoptotic genes are highly expressed at the base of…

DNA ComplementaryMolecular Sequence DataGene ExpressionApoptosisFresh WaterModels BiologicalConserved sequenceRussiaDemospongePhylogeneticsGene expressionCell polarityGeneticsAnimalsAmino Acid SequenceEF Hand MotifsMolecular BiologyGeneCaspaseConserved SequencePhylogenyCaspase 8Glutathione PeroxidasebiologySequence Homology Amino AcidEcologyCaspase 3Cell PolarityCell BiologyGeneral MedicineSequence Analysis DNAbiology.organism_classificationBlotting NorthernCell biologyPoriferaProtein Structure TertiarySpongeProto-Oncogene Proteins c-bcl-2Caspasesbiology.proteinDNA and cell biology
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A novel tunicate (Botryllus schlosseri) putative C-type lectin features an immunoglobulin domain.

1997

We have cloned a putative C-type lectin of Botryllus schlosseri [Ascidiacea], whose deduced protein of 333 amino acids features three building blocks: (i) a Greek-key motif signature at the amino-terminus, (ii) a C-type lectin domain signature, and (iii) an immunoglobulin (Ig) domain at the carboxyl terminus. This C-type lectin was termed BSCLT. Similarity searches revealed that the Ig domain in BSCLT, which is evidently not polymorphic, is best classified as an Intermediate-type Ig domain. Rabbit antibodies, raised against recombinant BSCLT, cross-reacted in a Western blot with a 38-kD polypeptide in tunicate crude extract. Presumably, this bimodal tunicate protein is the first description…

DNA ComplementaryMolecular Sequence DataImmunoglobulinsBotryllus schlosseriImmunoglobulin domainC-type lectinLectinsGeneticsAnimalsLectins C-TypeAmino Acid SequenceUrochordataMolecular Biologychemistry.chemical_classificationbiologyBase SequenceSequence Homology Amino AcidCD69LectinCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyAmino acidTunicateKLRB1chemistrybiology.proteinDNA and cell biology
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Increased Expression of Integrin and Receptor Tyrosine Kinase Genes During Autograft Fusion in the SpongeGeodia cydonium

1999

Recently cDNAs coding for cell surface molecules have been isolated from sponges. The molecules for alpha-integrin, galectin, and receptor tyrosine kinase (RTK), obtained from the marine sponge, Geodia cydonium, have been described earlier. In the present study also the cDNA for one putative beta-integrin has been identified from G. cydonium. The deduced aa sequence comprises the characteristic signatures, found in other metazoan beta-integrin molecules; the estimated size is 95,215 Da. To obtain first insights into the molecular events which proceed during autograft fusion, the expressions of these genes were determined on transcriptional and translational level. The cDNAs as well as antib…

DNA ComplementaryMolecular Sequence DataIntegrinGene ExpressionReceptor tyrosine kinaselaw.inventionlawTranscription (biology)Complementary DNAAnimalsHumansAmino Acid SequenceNorthern blotCloning MolecularGenePhylogenyGalectinBase SequenceSequence Homology Amino AcidStaining and LabelingbiologyIntegrin beta1Receptor Protein-Tyrosine KinasesGeneral MedicineMolecular biologyPoriferabiology.proteinRecombinant DNACell Adhesion and Communication
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