Search results for "sequence"

showing 10 items of 4987 documents

PCR survey ofXenoturbella bockiHox genes

2007

Xenoturbella bocki has recently been identified as one of the most basal deuterostomes, although an even more basal phylogenetic position cannot be ruled out. Here we report on a polymerase chain reaction survey of partial Hox homeobox sequences of X. bocki. Surprisingly, we did not find evidence for more than five Hox genes, one clear labial/PG1 ortholog, one posterior gene most similar to the PG9/10 genes of Ambulacraria, and three central group genes whose precise assignment to a specific paralog group remains open. We furthermore report on a re-evaluation of the available published evidence of Hox genes in other basal deuterostomes.

animal structuresBiologyDNA Ribosomallaw.inventionBasal (phylogenetics)lawGeneticsAnimalsAmino Acid SequenceAmbulacrariaHox geneGenePhylogenyEcology Evolution Behavior and SystematicsPolymerase chain reactionGeneticsPhylogenetic treeXenoturbella bockiGenes Homeoboxbiology.organism_classificationInvertebratesMultigene FamilyMolecular MedicineHomeoboxAnimal Science and ZoologyDevelopmental BiologyJournal of Experimental Zoology Part B: Molecular and Developmental Evolution
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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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Number, identity, and sequence of the Drosophila head segments as revealed by neural elements and their deletion patterns in mutants.

1994

The development of the insect head tagma involves massive rearrangements and secondary fusions of segment anlagen during embryogenesis. Due to the lack of reliable morphological markers, the number, identity, and sequence of the head segments, particularly in the pregnathal region, are still a matter of ongoing debates. We examined the complex array of internal structures of the embryonic Drosophila melanogaster head such as the sensory structures and nerves of the peripheral and stomatogastric nervous systems, and we used embryonic head mutations causing a lack of overlapping segment anlagen to unravel the segmental identity and the sequence of the neural elements. Our results provide evid…

animal structuresHead (linguistics)media_common.quotation_subjectMorphogenesisInsectPeripheral Nervous SystemMorphogenesisAnimalsDrosophila ProteinsDrosophila (subgenus)TagmaSequence (medicine)media_commonHomeodomain ProteinsGeneticsMultidisciplinarybiologyPhylogenetic treeGenes Homeoboxbiology.organism_classificationDrosophila melanogasterInsect HormonesImmunologic TechniquesDrosophila melanogasterHeadResearch ArticleTranscription FactorsProceedings of the National Academy of Sciences
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Regulatory sequences driving expression of the sea urchin Otp homeobox gene in oral ectoderm cells.

2005

Abstract PlOtp (Orthopedia), a homeodomain-containing transcription factor, has been recently characterized as a key regulator of the morphogenesis of the skeletal system in the embryo of the sea urchin Paracentrotus lividus . Otp acts as a positive regulator in a subset of oral ectodermal cells which transmit short-range signals to the underlying primary mesenchyme cells where skeletal synthesis is initiated. To shed some light on the molecular mechanisms involved in such a process, we begun a functional analysis of the cis -regulatory sequences of the Otp gene. Congruent with the spatial expression profile of the endogenous Otp gene, we found that while a DNA region from −494 to +358 is s…

animal structuresMesenchymeTransgeneGreen Fluorescent ProteinsEctodermSettore BIO/11 - Biologia MolecolareBiologyGreen fluorescent proteinAnimals Genetically ModifiedEctodermGeneticsmedicineAnimalsRNA MessengerMolecular BiologyGeneTranscription factorSea urchin development Skeletogenesis Orthopedia homeobox gene Oral ectoderm microinjectionHomeodomain ProteinsBase SequenceGenes HomeoboxGene Expression Regulation DevelopmentalDNAMolecular biologyRecombinant Proteinsmedicine.anatomical_structureRegulatory sequenceembryonic structuresParacentrotusHomeoboxDigestive SystemDevelopmental BiologyTranscription FactorsGene expression patterns : GEP
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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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