Search results for " Homology"

showing 10 items of 633 documents

Termite Gut Symbiotic Archaezoa Are Becoming Living Metabolic Fossils

2003

ABSTRACT Over the course of several million years, the eukaryotic gut symbionts of lower termites have become adapted to a cellulolytic environment. Up to now it has been believed that they produce nutriments using their own cellulolytic enzymes for the benefit of their termite host. However, we have now isolated two endoglucanases with similar apparent molecular masses of approximately 36 kDa from the not yet culturable symbiotic Archaezoa living in the hindgut of the most primitive Australian termite, Mastotermes darwiniensis . The N-terminal sequences of these cellulases exhibited significant homology to cellulases of termite origin, which belong to glycosyl hydrolase family 9. The corre…

DNA ComplementaryMolecular Sequence DataIsopteraCellulaseMicrobiologySalivary GlandsArticleMicrobiologySymbiosisPhylogeneticsMastotermes darwiniensisHydrolaseAnimalsCellulasesAmino Acid SequenceFlagellateSymbiosisMolecular BiologyGenePhylogenyCell NucleusSequence Homology Amino AcidbiologyEukaryotaHindgutSequence Analysis DNAGeneral Medicinebiology.organism_classificationGastrointestinal Tractbiology.proteinEukaryotic Cell
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Evolutionary relationships of the metazoan βγ–crystallins, including that from the marine spongeGeodia cydonium

1997

beta gamma-crystallins are one major component of vertebrate lenses. Here the isolation and characterization of a cDNA, coding for the first beta gamma-crystallin molecule from an invertebrate species, the marine sponge Geodia cydonium, is described. The size of the transcript as determined by Northern blotting was 0.7 kb in length. The deduced amino acid sequence consists of 163 aa residues and comprises four repeated motifs which compose the two domains of the beta gamma-crystallin. Motif 3 contains the characteristic beta gamma-crystallin 'Greek key' motif signature, while in each of the three other repeats, one aa residue is replaced by an aa with the same physico-chemical property. The…

DNA ComplementaryMolecular Sequence DataPhysarum polycephalumSequence alignmentPolymerase Chain ReactionGeneral Biochemistry Genetics and Molecular BiologyEvolution MolecularFungal ProteinsPhysarum polycephalumPhylogeneticsComplementary DNAAnimalsHumansAmino Acid SequencePeptide sequencePhylogenyDNA PrimersGene LibraryGeneral Environmental Sciencechemistry.chemical_classificationGeneticsFungal proteinBase SequenceSequence Homology Amino AcidGeneral Immunology and MicrobiologybiologyCoccidioidinGeneral Medicinebiology.organism_classificationCrystallinseye diseasesPoriferaAmino acidSpongechemistryEvolutionary biologysense organsGeneral Agricultural and Biological SciencesSequence AlignmentResearch ArticleProceedings of the Royal Society of London. Series B: Biological Sciences
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Experimental indication in favor of the introns-late theory: the receptor tyrosine kinase gene from the sponge Geodia cydonium.

1997

Abstract We have analyzed the gene that encodes receptor tyrosine kinase (RTK) from the marine sponge Geodia cydonium, which belongs to the most ancient and simple metazoan groups, the Porifera. RTKs are enzymes found only in metazoa. The sponge gene contains two introns in the extracellular part of the protein. However, the rest of the protein (transmembrane and intracellular part), including the tyrosine kinase (TK)-domain, is encoded by a single exon. In contrast, all TK genes, so far known only from higher animals (vertebrates), contain several introns especially in the TK-domain. The TK-domain of G. cydonium shows similarity with numerous members of receptor as well as nonreceptor TKs.…

DNA ComplementaryMolecular Sequence DataReceptor tyrosine kinaseCatalysisExonSequence Homology Nucleic AcidGeneticsAnimalsHumansReceptor Tyrosine Kinase GeneAmino Acid SequenceCloning MolecularIntrons; Evolution; Tyrosine kinases; SpongesMolecular BiologyIntracellular partGeneEcology Evolution Behavior and SystematicsPhylogenyGeneticsbiologyPhylogenetic treeBase SequenceSequence Homology Amino AcidIntronReceptor Protein-Tyrosine KinasesIntronsPoriferaBiochemistrybiology.proteinTyrosine kinaseJournal of molecular evolution
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Molecular cloning of a tyrosine kinase gene from the marine spongeGeodia cydonium: a new member belonging to the receptor tyrosine kinase class II fa…

1994

We have isolated and characterized a cDNA from the marine sponge Geodia cydonium coding for a new member of the tyrosine protein kinase (TK) family. The cDNA encodes a protein of M(r) = 68,710, termed GCTK, which is homologous to class II receptor tyrosine kinases (RTKs). GCTK contains conserved amino acids (aa) characteristic of all protein kinases, and the sequences DLATRN and PIRWMATE which are highly specific for TKs. Furthermore, the sequence N-L-Y-x(3)-Y-Y-R is highly homologous to the sequence D-[LIV]-Y-x(3)-Y-Y-R found only in class II RTKs. The sponge TK, when compared with mammalian class II RTKs, shows maximum 31% homology in the TK domain indicating that this the oldest member o…

DNA ComplementaryMolecular Sequence DataReceptor tyrosine kinaseSH3 domainCytosolAnimalsGeodiaAmino Acid SequenceRNA MessengerCloning MolecularKinase activityTyrosineProtein kinase AMolecular BiologyBase SequenceSequence Homology Amino AcidbiologyCell MembraneReceptor Protein-Tyrosine KinasesCell BiologyProtein-Tyrosine Kinasesbiology.organism_classificationBiological EvolutionMolecular biologyPoriferaMolecular WeightBiochemistryROR1biology.proteinTyrosine kinaseMolecular Membrane Biology
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Tonoplast subcellular localization of maize cytochrome b5 reductases

2000

Plant cytochrome b 5 reductases (b 5 R) are assumed to be part of an ER-associated redox chain that oxidizes NADH to provide electrons via cytochrome b5 (cyt b 5 ) to ER-associated fatty acyl desaturase and related hydroxylases, as in mammalian cells. Here we report on cDNA cloning of a novel maize b 5 R, NFR II, strongly related to a previously cloned cDNA, NFR I (Bagnaresi et al., 1999, Biochem, J. 338, 499-5051. Maize b 5 R isoforms are produced by a small multi-gene family. The NFR cDNAs were shown to encode active b 5 Rs by heterologous expression in yeast. Both reductases, in addition to Fe 3+ -chelates, efficiently reduced Cu 2+ -chelates. Using a polyclonal antibody able to recogniz…

DNA ComplementaryMolecular Sequence DataSaccharomyces cerevisiaePlant ScienceMolecular cloningBiologyPlant RootsZea maysIsozymeGene Expression Regulation EnzymologicComplementary DNACytochrome b5GeneticsAmino Acid SequenceMicroscopy ImmunoelectronCytochrome ReductasesCytochrome b5 reductaseSequence Homology Amino AcidCytochrome bSequence Analysis DNACell BiologySubcellular localizationMolecular biologyIsoenzymesBiochemistryVacuolesHeterologous expressionSequence AlignmentCytochrome-B(5) ReductaseThe Plant Journal
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Identification of a gene overexpressed in aphids reared under short photoperiod.

2003

Most aphids develop a cyclic parthenogenesis life-cycle. After several generations of viviparously produced parthenogenetic females, follows a single annual generation of sexual individuals, usually in autumn, that mate and lay the sexual eggs. Shortening of photoperiod at the end of the summer (together with temperature) is a key factor inducing the sexual response. Currently no genes involved in the cascade of events that lead to the appearance of sexual forms have been reported. After a Differential Display RT-PCR survey performed on Acyrthosiphon pisum aphids, we identified a gene that is overexpressed in aphids reared under short photoperiod conditions that induce sexuality in this spe…

DNA ComplementaryPhotoperiodMolecular Sequence DataBiologyBiochemistrySexual Behavior AnimalComplementary DNAAnimalsCircadian rhythmAmino Acid SequenceCloning MolecularMolecular BiologyGeneDNA PrimersphotoperiodismGeneticsDifferential displayBase SequenceSequence Homology Amino Acidfood and beveragesParthenogenesisbiology.organism_classificationAcyrthosiphon pisumInsect ScienceAphidsGABAergicInsect ProteinsInsect biochemistry and molecular biology
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γ-Tubulin in Barley and Tobacco: Sequence Relationship and RNA Expression Patterns in Developing Leaves during Mitosis and Post-Mitotic Growth

2002

gamma-Tubulin is typically associated with microtubule organising centres, such as the centrosome, and appears to mediate microtubule nucleation. Centrosomes are usually not found in higher plants, but active genes homologous to gamma-tubulin have been identified in the plant kingdom, including the angiosperms Arabidopsis, maize and rice. We have isolated and characterised gamma-tubulin cDNA sequences of two further angiosperm species, barley and tobacco. Sequence comparison revealed a phylogenetic tree with distinct clusters corresponding to the systematic position of the species. Furthermore, domains, thought to be exposed in the folded protein and to be candidates for interaction with as…

DNA ComplementaryPhysiologyMolecular Sequence DataMitosismacromolecular substancesPlant ScienceGene Expression Regulation PlantTubulinMicrotubuleTobaccoAmino Acid SequenceGeneMitosisPhylogenyMicrotubule nucleationGeneticsSequence Homology Amino AcidbiologyGene Expression Regulation Developmentalfood and beveragesRNAHordeumCell BiologyGeneral MedicineBlotting NorthernCell biologyPlant LeavesTubulinRNA PlantCentrosomebiology.proteinCortical microtubulePlant and Cell Physiology
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Putative phenoloxidases in the tunicate Ciona intestinalis and the origin of the arthropod hemocyanin superfamily.

2003

In addition to the respiratory copper-containing proteins for which it is named, the arthropod hemocyanin superfamily also includes phenoloxidases and various copperless storage proteins (pseudo-hemocyanins, hexamerins and hexamerin receptors). It had long been assumed that these proteins are restricted to the arthropod phylum. However, in their analysis of the predicted genes in the Ciona intestinalis (Urochordata:Tunicata) genome, Dehal et al. (Science 298:2157–2167) proposed that the sea squirt lacks hemoglobin but uses hemocyanin for oxygen transport. While there are, nevertheless, four hemoglobin genes present in Ciona, we have identified and cloned two cDNA sequences from Ciona that i…

DNA ComplementaryPhysiologymedicine.medical_treatmentMolecular Sequence Datachemical and pharmacologic phenomenacomplex mixturesBiochemistryEvolution MolecularEndocrinologyPhylogeneticsmedicineAnimalsCiona intestinalisAmino Acid SequenceArthropodsEcology Evolution Behavior and SystematicsPhylogenybiologyBase SequenceSequence Homology Amino AcidMonophenol MonooxygenaseOxygen transportHemocyaninAnatomybiology.organism_classificationCiona intestinalisCionaEvolutionary biologyHemocyaninsAnimal Science and ZoologyArthropod ProteinsArthropodOxygen bindingJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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Identification, molecular cloning, and phylogenetic analysis of a non-respiratory pseudo-hemocyanin of Homarus americanus.

1999

Copper-containing hemocyanins serve to transport oxygen in many arthropod species. Here I describe the identification and cDNA cloning of a structurally closely related non-respiratory pseudo-hemocyanin (PHc) of the American lobster, Homarus americanus. This protein has lost the ability to bind copper and, therefore, oxygen because a histidine residue in copper-binding site A is replaced by tyrosine. Like many arthropod hemocyanins, PHc forms a hexamer. It consists of two different subunit types of 660 and 661 amino acids, respectively, that share a 94.4% sequence identity. Whereas Homarus hemocyanin is produced in the hepatopancreas, PHc is synthesized by the ovaries and the heart tissue. …

DNA ComplementaryProtein subunitmedicine.medical_treatmenteducationMolecular Sequence Datachemical and pharmacologic phenomenaMolecular cloningBiologybehavioral disciplines and activitiesBiochemistryPhylogeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequencePhylogenychemistry.chemical_classificationHomarusBase SequenceSequence Homology Amino AcidEcologyHemocyaninCell BiologyProtein superfamilybiology.organism_classificationAmino acidNephropidaeMicroscopy ElectronBiochemistrychemistryHemocyaninsThe Journal of biological chemistry
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Tumor suppression inDrosophila is causally related to the function of thelethal(2)tumorous imaginal discs gene, adnaJ homolog

1995

The Drosophila melanogaster tumor suppressor gene lethal(2)tumorous imaginal discs (l(2)tid) causes in homozygotes malignant growth of cells of the imaginal discs and the death of the mutant larvae at the time of puparium formation. We describe the molecular cloning of the l(2)tid+ gene and its temporal expression pattern in the wild-type and mutant alleles. Germ line rescue of the tumor phenotype was achieved with a 7.0 kb Hindlll-fragment derived from the polytene chromosome band 59F5. The l(2)tid+ gene spans approximately 2.5 kb of genomic DNA. The protein coding region, 1,696 bps long, is divided by an intron into two exons. The predicted Tid56 protein contains 518 amino acids and posse…

DNA ComplementarySaccharomyces cerevisiae ProteinsTumor suppressor geneMolecular Sequence DataMutantGenes InsectSaccharomyces cerevisiaeAnimals Genetically ModifiedFungal ProteinsMitochondrial ProteinsSpecies SpecificityEscherichia coliGeneticsAnimalsDrosophila ProteinsHumansGenes Tumor SuppressorAmino Acid SequenceCloning MolecularGeneAllelesHeat-Shock ProteinsPolytene chromosome bandBase SequenceSequence Homology Amino AcidbiologyEscherichia coli ProteinsPupaChromosome MappingExonsNeoplasms ExperimentalCell BiologyHSP40 Heat-Shock Proteinsbiology.organism_classificationMolecular biologyImaginal discDrosophila melanogasterLarvaDNAJA2Drosophila melanogasterSequence AlignmentDrosophila ProteinDevelopmental BiologyDevelopmental Genetics
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