Search results for "sequence data"

showing 10 items of 1952 documents

Rat tyrosine kinase inhibitor shows sequence similarity to human α2-HS glycoprotein and bovine fetuin

1991

Human alpha 2-HS glycoprotein and bovine fetuin, abundant proteins of fetal plasma, are structural members of the fetuin family within the cystatin superfamily. They are characterized by the presence of two N-terminally located cystatin-like units and a unique C-terminal sequence segment not present in the other members of the cystatin superfamily. Search for related sequences revealed that the natural inhibitor of the insulin receptor tyrosine kinase [Auberger, Falquerho, Contreres, Pages, Le Cam, Rossi & Le Cam (1989) Cell (Cambridge, Mass.) 58, 631-640] shows sequence similarity to the mammalian fetuins. The sequence identity between rat tyrosine kinase inhibitor, human alpha 2-HS gl…

alpha-2-HS-Glycoproteinmedicine.drug_classMolecular Sequence DataBiochemistryTyrosine-kinase inhibitorReceptor tyrosine kinaseHomology (biology)Protein structureSequence Homology Nucleic AcidmedicineAnimalsHumansAmino Acid SequenceMolecular Biologychemistry.chemical_classificationbiologyBlood ProteinsCell BiologyProtein-Tyrosine KinasesMolecular biologyFetuinRatschemistryBiochemistrybiology.proteinCattlealpha-FetoproteinsGlycoproteinSequence Alignmentalpha-2-HS-glycoproteinResearch ArticleCysteineBiochemical Journal
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Okadaic Acid, an Apoptogenic Toxin for Symbiotic/Parasitic Annelids in the Demosponge Suberites domuncula

2006

ABSTRACT The role of okadaic acid (OA) in the defense system of the marine demosponge Suberites domuncula against symbiotic/parasitic annelids was examined. Bacteria within the mesohyl produced okadaic acid at concentrations between 32 ng/g and 58 ng/g of tissue (wet weight). By immunocytochemical methods and by use of antibodies against OA, we showed that the toxin was intracellularly stored in vesicles. Western blotting experiments demonstrated that OA also existed bound to a protein with a molecular weight of 35,000 which was tentatively identified as a galectin (by application of antigalectin antibodies). Annelids that are found in S. domuncula undergo apoptotic cell death. OA is one ca…

animal structuresAnnelidaMolecular Sequence DataApoptosismedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologychemistry.chemical_compoundOkadaic AcidInvertebrate MicrobiologymedicineAnimalsHumansMesohylAmino Acid SequenceSymbiosisGalectinAnnelidBacteriaEcologybiologyToxinOkadaic acidbiology.organism_classificationDNA-Binding ProteinsSuberites domunculachemistryBiochemistrySuberitesBacteriaTranscription FactorsFood ScienceBiotechnologySuberitesApplied and Environmental Microbiology
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Tracing the origin of the compensasome: evolutionary history of DEAH helicase and MYST acetyltransferase gene families.

2001

Dosage compensation in Drosophila is mediated by a complex of proteins and RNAs called the "compensasome." Two of the genes that encode proteins of the complex, maleless (mle) and males-absent-on-the-first (mof), respectively, belong to the DEAH helicase and MYST acetyltransferase gene families. We performed comprehensive phylogenetic and structural analyses to determine the evolutionary histories of these two gene families and thus to better understand the origin of the compensasome. All of the members of the DEAH and MYST families of the completely sequenced Saccharomyces cerevisiae and Caenorhabditis elegans genomes, as well as those so far (June 2000) found in Drosophila melanogaster (f…

animal structuresChromosomal Proteins Non-HistoneMolecular Sequence DataBiologyEvolution MolecularAcetyltransferasesGeneticsGene familyAnimalsDrosophila ProteinsAmino Acid SequenceMolecular BiologyGeneEcology Evolution Behavior and SystematicsCaenorhabditis elegansPhylogenyHistone AcetyltransferasesGeneticsDosage compensationSequence Homology Amino AcidfungiDNA HelicasesHelicaseNuclear Proteinsbiology.organism_classificationRNA Helicase ACaenorhabditisDNA-Binding ProteinsMultigene Familybiology.proteinDrosophila melanogasterRNA HelicasesTranscription FactorsMolecular biology and evolution
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Spatially restricted expression of PlOtp, a Paracentrotus lividus Orthopedia-related homeobox gene, is correlated with oral ectodermal patterning and…

1999

ABSTRACT Several homeobox genes are expressed in the sea urchin embryo but their roles in development have yet to be elucidated. Of particular interest are homologues of homeobox genes that in mouse and Drosophila are involved in patterning the developing central nervous system (CNS). Here, we report the cloning of an orthopedia (Otp)-related gene from Paracentrotus lividus, PlOtp. Otp is a single copy zygotic gene that presents a unique and highly restricted expression pattern. Transcripts were first detected at the mid-gastrula stage in two pairs of oral ectoderm cells located in a ventrolateral position, overlying primary mesenchyme cell (PMC) clusters. Increases in both transcript abund…

animal structuresDNA ComplementaryStomodeumBody PatterningPolarity in embryogenesisCell specificationCleavage Stage OvumMolecular Sequence DataGene DosageGene ExpressionSettore BIO/11 - Biologia MolecolareEctodermNerve Tissue ProteinsParacentrotus lividusGene expressionEctodermmedicineAnimalsDrosophila ProteinsAmino Acid SequenceCloning MolecularMolecular BiologyBody PatterningGeneticsHomeodomain ProteinsbiologyBase SequenceGenes HomeoboxOrthopediaSequence Analysis DNAbiology.organism_classificationCell biologymedicine.anatomical_structureEctopic expressionParacentrotus lividusSea UrchinsSpiculogenesisSettore BIO/03 - Botanica Ambientale E Applicataembryonic structuresHomeoboxEctopic expressionDevelopmental Biology
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Bruton tyrosine kinase-like protein, BtkSD, is present in the marine sponge Suberites domuncula.

2003

Sponges, the simplest and most ancient phylum of Metazoa, encode in their genome complex and highly sophisticated proteins that evolved together with multicellularity and are found only in metazoan animals. We report here the finding of a Bruton tyrosine kinase (BTK)-like protein in the marine sponge Suberites domuncula (Demospongiae). The nucleotide sequence of one sponge cDNA predicts a 700-aa-long protein, which contains all of the characteristic domains for the Tec family of protein tyrosine kinases (PTKs). The highest homology (38% identity, 55% overall similarity) was found with human BTK and TEC PTKs. Sponge PTK was therefore named BtkSD. Human BTK is involved in the maturation of B …

animal structuresDNA ComplementaryeducationMolecular Sequence DataHomology (biology)immune system diseaseshemic and lymphatic diseasesComplementary DNAGeneticsAgammaglobulinaemia Tyrosine KinaseBruton's tyrosine kinaseAnimalsHumansAmino Acid SequenceProtein kinase ACaenorhabditis elegansGeneCaenorhabditis elegansGeneticsbiologySequence Homology Amino AcidKinaseProtein-Tyrosine Kinasesbiology.organism_classificationPoriferaSuberites domunculaMutationbiology.proteinGenomics
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A galectin links the aggregation factor to cells in the sponge (Geodia cydonium) system.

1996

The cDNA for the full-length lectin from the marine sponge Geodia cydonium was cloned. Analysis of the deduced aa sequence revealed that this lectin belongs to the group of galectins. The full-length galectin, which was obtained also in a recombinant form, has an M(r) of 20,877; in the processed form it is a 15 kDa polypeptide. The enriched aggregation factor from G.cydonium also was determined to contain, besides minimal amounts of the galectin, a 140 kDa polypeptide which is involved in cell-cell adhesion. Monoclonal antibodies have been raised against this protein; Fab' fragments prepared from them abolished cell-cell reaggregation. Cell reaggregation experiments revealed that the aggreg…

animal structuresDNA Complementarymedicine.drug_classGalectinsCellMolecular Sequence DataMonoclonal antibodyBiochemistrylaw.inventionlawComplementary DNALectinsotorhinolaryngologic diseasesmedicineAnimalsAmino Acid SequenceCloning MolecularCell adhesionGalectinCell AggregationbiologyBase SequenceChemistryLectinAntibodies MonoclonalPoriferastomatognathic diseasesmedicine.anatomical_structureBiochemistrybiology.proteinRecombinant DNAAntibodyCell Adhesion MoleculesProtein BindingGlycobiology
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Study of the aminopeptidase N gene family in the lepidopterans Ostrinia nubilalis (Hübner) and Bombyx mori (L.): Sequences, mapping and expression

2010

Aminopeptidases N (APNs) are a class of ectoenzymes present in lepidopteran larvae midguts, involved in the Bacillus thuringiensis (Bt) toxins mode of action. In the present work, seven aminopeptidases have been cloned from the midgut of Ostrinia nubilalis, the major Lepidopteran corn pest in the temperate climates. Six sequences were identified as APNs because of the presence of the HEXXH(X)18E and GAMEN motifs, as well as the signal peptide and the GPI-anchor sequences. The remaining sequence did not contain the two cellular targeting signals, indicating it belonged to the puromycin-sensitive aminopeptidase (PSA) family. An in silico analysis allowed us to find orthologous sequences in Bo…

animal structuresGenetic LinkageSequence analysisMolecular Sequence DataSettore BIO/05 - ZoologiaSequence alignmentBt toxin-binding proteinCD13 AntigensMothsBiochemistryAminopeptidaseOstriniaPuromycin-Sensitive AminopeptidaseQuantitative PCRMidgut APNSequence Analysis ProteinBombyx moriSequence Homology Nucleic AcidBacillus thuringiensisAnimalsAmino Acid SequenceRNA MessengerCloning MolecularMolecular BiologyGenePhylogenyGeneticsbiologyLarval development expressionGene Expression ProfilingfungiComputational BiologyBombyxbiology.organism_classificationMolecular biologyIsoenzymesSettore BIO/18 - GeneticaSettore AGR/11 - Entomologia Generale E ApplicataLarvaMultigene FamilyInsect ScienceInsect ProteinsPuromycin-sensitive aminopeptidaseSequence Alignment
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Neuroglobin, cytoglobin, and a novel, eye-specific globin from chicken

2004

Neuroglobin and cytoglobin are two recently discovered respiratory proteins of vertebrates. Here we report the first identification and expression analyses of these proteins in bird species. Neuroglobin from the domestic chicken Gallus gallus differs in approximately 30% from the mammalian proteins, but its genome structure shows the conservation of the B12.2, E11.0, and G7.0 intron positions. The chicken cytoglobin protein is shorter than the mammalian orthologs, from which it differs overall by approximately 25%, due to the absence of the C-terminal exon in the gene. Comparison of chicken and mammalian gene order shows that neuroglobin and cytoglobin are located on conserved syntenic chro…

animal structuresMolecular Sequence DataBiophysicsNeuroglobinNerve Tissue ProteinsBiologyBiochemistryRetinaEvolution MolecularExonSpecies SpecificitySequence Analysis ProteinGene duplicationAnimalsHumansAmino Acid SequenceGlobinMolecular BiologyGeneConserved SequencePhylogenyGeneticsSequence Homology Amino AcidCytoglobinIntronRNACell BiologyGlobinsNeuroglobinVertebratesChickensBiochemical and Biophysical Research Communications
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Globin genes are present in Ciona intestinalis.

2003

The key position of the Ciona intestinalis basal to the vertebrate phylogenetic tree brings up the question of which respiratory proteins are used by the tunicate to facilitate oxygen transport and storage. The publication of the Ciona draft genome sequence suggests that globin genes are completely missing and that-like some molluscs and arthropods-the sea squirt uses hemocyanin instead of hemoglobin for respiration. However, we report here the presence and expression of at least four distinct globin gene/protein sequences in Ciona. This finding is in agreement with the ancestral phylogeny of the vertebrate globins. Moreover, it seems likely that the Ciona hemocyanin-like sequences have enz…

animal structuresMolecular Sequence DataGenomeEvolution MolecularPhylogeneticsGeneticsAnimalsCiona intestinalisGlobinAmino Acid SequenceMolecular BiologyEcology Evolution Behavior and SystematicsPhylogenyWhole genome sequencingGeneticsGenomebiologyPhylogenetic treeSequence Homology Amino AcidfungiOxygen transportAnatomybiology.organism_classificationCiona intestinalisGlobinsCionaembryonic structuresMolecular biology and evolution
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The organization, localization and nucleotide sequence of the histone genes of the midge Chironomus thummi.

1991

Several histone gene repeating units containing the genes for histones H1, H2A, H2B, H3 and H4 were isolated by screening a genomic DNA library from the midge Chironomus thummi ssp. thummi. The nucleotide sequence of one complete histone gene repeating unit was determined. This repeating unit contains one copy of each of the five histone genes in the order and orientation mean value of H3 H4 mean value of H2A H2B H1 mean value of. The overall length is 6262 bp. The orientation, nucleotide sequence and inferred amino acid sequence as well as the chromosomal arrangement and localization are different from those reported for Drosophila melanogaster. The codon usage also shows marked difference…

animal structuresMolecular Sequence DataRestriction MappingChironomidaeHistone H4HistonesHistone H3Histone H1Species SpecificityHistone H2AGeneticsHistone H2BAnimalsAmino Acid SequenceCodonPeptide sequenceGenetics (clinical)Repetitive Sequences Nucleic AcidGeneticsbiologyBase SequencefungiNucleic acid sequenceDNAHistoneDrosophila melanogasterbiology.proteinChromosoma
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