Search results for "Sequence alignment"

showing 10 items of 447 documents

A novel serine/threonine kinase gene, STK33 , on human chromosome 11p15.3

2001

Human chromosomal region 11p15 is known to be associated with several diseases including predispositions to develop various tumor types. In search of candidate genes, a novel human kinase gene is described, STK33, which codes for a serine/threonine protein kinase. The gene was discovered by comparative genome analysis of human chromosome 11p15.3 and its orthologous region on distal mouse chromosome 7. Human STK33 gene contains 12 exons as has been determined by the comparison to the full-length transcript amplified from human uterus RNA. Transcripts are found in a variety of tissues in at least two alternatively spliced forms as revealed by reverse transcriptase-polymerase chain reaction, c…

MaleDNA ComplementaryMolecular Sequence DataGene ExpressionProtein Serine-Threonine KinasesMAP3K7MAP2K7MiceTANK-binding kinase 1GeneticsAnimalsHumansTissue DistributionAmino Acid SequenceRNA Messengerc-RafPhylogenyGeneticsSerine/threonine-specific protein kinaseBase SequenceSequence Homology Amino AcidbiologyChromosomes Human Pair 11Cyclin-dependent kinase 2DNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsGenesChromosomal regionbiology.proteinFemalePRKCB1Sequence AlignmentGene
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Molecular characterization of Lma-p54, a new epicuticular surface protein in the cockroach Leucophaea maderae (Dictyoptera, oxyhaloinae)

2002

0965-1748 (Print) Journal Article Research Support, Non-U.S. Gov't; The epicuticular surface protein Lma-p54 is imbedded in the "cuticular waxes" which cover the abdominal surface of the adult Leucophaea maderae. Natural Lma-p54 was purified and the complete cDNA sequence was determined by RT-PCR using primers based on Edman degradation fragments. Northern blot and in situ hybridization analyses showed that Lma-p54 was expressed in the adult abdominal epidermis and in the chemical sense organs of both sexes. Sequence alignment indicates that Lma-p54 is closely related to aspartic proteases (EC 3.4.23). However, there are critical amino acid substitutions at the level of the active site and,…

MaleDNA ComplementaryMolecular Sequence DataSequence HomologyCockroachesSequence alignmentRecombinant Proteins/chemistryComplementary/geneticsBiochemistryPolymerase Chain ReactionCockroaches/*genetics/growth & developmentComplementary DNAAspartic Endopeptidases/*geneticsAspartic Acid EndopeptidasesAnimalsGlycoproteins/*geneticsNorthern blotAmino Acid SequenceMolecular BiologyPeptide sequenceIn Situ HybridizationGlycoproteinschemistry.chemical_classificationSequence Homology Amino AcidbiologyEdman degradationBase SequenceDictyopteraDNAbiology.organism_classificationMolecular biologyRecombinant ProteinsAmino acidInsect Proteins/*geneticsAmino AcidBiochemistrychemistryInsect ScienceLarvaInsect ProteinsFemaleGlycoproteinSequence Alignment
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Isolation and characterization of cold-shock domain protein genes, Oryzias latipes Y-box protein 2 ( OlaYP2 ) and Fugu rubripes Y-box protein 1 ( Fru…

2002

The Y-box protein (YP) family shares a nucleic acid binding domain, called cold-shock domain, that has been evolutionarily highly conserved from bacteria to human. The different YPs identified so far in vertebrates are thought to function as transcriptional activators, transcriptional repressors and/or translational repressors. Medakafish and pufferfish are very suitable vertebrate models for the study of developmental genetics and comparative genomics, respectively. Here we report the isolation of two teleost YP genes, medakafish Oryzias latipes (Ola)YP2 and Fugu rubripes (Fru)YP1, which are expressed in multiple tissues. Phylogenetic analysis demonstrated that OlaYP2 and FruYP1 belong to …

MaleDNA ComplementarySequence analysisOryziasMolecular Sequence DataProtein domainOryziasGene ExpressionBiologyGeneticsAnimalsAmino Acid SequenceIn Situ Hybridization FluorescencePhylogenyComparative genomicsGeneticsBase SequenceSequence Homology Amino AcidFugufungiChromosome MappingSequence Analysis DNAGeneral MedicineY box binding protein 1Cold-shock domainbiology.organism_classificationTakifuguFemaleSequence AlignmentTranscription FactorsBinding domainGene
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The new gene DmX from Drosophila melanogaster encodes a novel WD-repeat protein

1998

DmX is a novel gene from Drosophila melanogaster located on the X chromosome in region 5D5/6-E1. The molecular analysis of the genomic and cDNA sequences of DmX shows that the gene spans appr. 16kb and displays a mosaic structure with 15 exons. The 12kb long DmX transcript is present in Drosophila embryos, larvae and adults of both sexes. The open reading frame of DmX encodes a novel WD-repeat protein, containing at least 30 WD-repeat units. WD-repeat proteins contain a conserved motif of approximately 40 amino acids (aa), usually ending with the dipeptide Trp-Asp (WD). Homologues of the DmX gene exist in other dipteran species, in Caenorhabditis elegans and human, revealing that DmX is an …

MaleDNA ComplementaryX ChromosomeTranscription GeneticMolecular Sequence DataGenes InsectOpen Reading FramesExonComplementary DNAGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerCloning MolecularPeptide sequenceGeneConserved SequenceX chromosomeCaenorhabditis elegansRepetitive Sequences Nucleic AcidGeneticsAspartic AcidbiologyTryptophanChromosome MappingGene Expression Regulation DevelopmentalSequence Analysis DNAGeneral Medicinebiology.organism_classificationOpen reading frameDrosophila melanogasterInsect ProteinsFemaleDrosophila melanogasterSequence AlignmentGene
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Molecular cloning and characterization of the cDNA encoding the rat liver gamma-butyrobetaine hydroxylase

1999

Carnitine biosynthesis from lysine and methionine involves five enzymatic reactions. gamma-butyrobetaine hydroxylase (BBH; EC 1.14. 11.1) is the last enzyme of this pathway. It catalyzes the reaction of hydroxylation of gamma-butyrobetaine to carnitine. The cDNA encoding this enzyme has been isolated and characterized. The cDNA contained an open reading frame of 1161 bp encoding a protein of 387 amino acids with a deduced molecular weight of 44.5 kDa. The sequence of the cDNA showed an important homology with the human cDNA recently isolated. Northern analysis showed gamma-butyrobetaine hydroxylase expression in the liver and in some extend in the testis and the epididymis. During this stud…

MaleDNA Complementarygamma-Butyrobetaine DioxygenaseMolecular Sequence DataBiologyMolecular cloningMixed Function Oxygenaseschemistry.chemical_compoundSequence Homology Nucleic AcidComplementary DNAmedicineAnimalsAmino Acid SequenceCarnitineCloning MolecularRats WistarMolecular Biologychemistry.chemical_classificationMessenger RNAMethionineBase SequenceSequence Homology Amino AcidGene Expression Regulation DevelopmentalCell BiologyMolecular biologyRatsAmino acidOpen reading frameLiverchemistryBiochemistryCarnitine biosynthesisSequence Alignmentmedicine.drugBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Mutations inWNT10Aare frequently involved in oligodontia associated with minor signs of ectodermal dysplasia

2012

Ectodermal dysplasias (ED) are a clinically and genetically heterogeneous group of hereditary disorders that have in common abnormal development of ectodermal derivatives. Hypohidrotic ectodermal dysplasia (HED) is characterized by abnormal development of eccrine sweat glands, hair, and teeth. The X-linked form of the disease, caused by mutations in the EDA gene, represents the majority of patients with the hypohidrotic form. Autosomal dominant and autosomal recessive forms are occasionally seen, and result from mutations in at least three genes (WNT10A, EDAR, or more rarely EDARADD). We have screened for mutations in EDAR (commonly involved in the hypohidrotic form) and WNT10A (involved in…

MaleEctodermal dysplasiaGenotypeMolecular Sequence Datamedicine.disease_causeCompound heterozygosityEctodermal DysplasiaGeneticsmedicineHumansAmino Acid SequenceHypohidrotic ectodermal dysplasiaGenetic Association StudiesGenetics (clinical)AnodontiaGeneticsMutationEDARADDEdar ReceptorGenetic heterogeneitybusiness.industrymedicine.diseaseWnt ProteinsHypodontiaPhenotypeMutationFemaleEctodysplasin AbusinessSequence AlignmentAmerican Journal of Medical Genetics Part A
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Visualization of a covalent intermediate between microsomal epoxide hydrolase, but not cholesterol epoxide hydrolase, and their substrates

1997

Mammalian soluble and microsomal epoxide hydrolases have been proposed to belong to the family of alpha/beta-hydrolase-fold enzymes. These enzymes hydrolyse their substrates by a catalytic triad, with the first step of the enzymatic reaction being the formation of a covalent enzyme-substrate ester. In the present paper, we describe the direct visualization of the ester formation between rat microsomal epoxide hydrolase and its substrate. Microsomal epoxide hydrolase was precipitated with acetone after brief incubation with [1-(14)C]epoxystearic acid. After denaturing SDS gel electrophoresis the protein-bound radioactivity was detected by fluorography. Pure epoxide hydrolase and crude micros…

MaleEpoxide hydrolase 21303 BiochemistryStereochemistryMolecular Sequence DataEpoxide10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiochemistryRats Sprague-Dawleychemistry.chemical_compoundCatalytic triadAnimalsAmino Acid SequenceEpoxide hydrolaseMolecular BiologyEpoxide Hydrolaseschemistry.chemical_classificationHydrolysisCell BiologyRatsKineticsCholesterolEnzymeModels ChemicalSolubilitychemistryBiochemistryMicrosomal epoxide hydrolaseEpoxide HydrolasesCarcinogensChromatography GelMicrosomes LiverMicrosomeEpoxy Compounds570 Life sciences; biologySequence AlignmentStearic Acids
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Echinostoma caproni: identification of enolase in excretory/secretory products, molecular cloning, and functional expression.

2007

In order to investigate molecules that could be involved in host-trematode relationships, we have analysed the excretory/secretory products (ESP) of Echinostoma caproni following a proteomic approach. Actin, Gluthathione S-transferase (GST) and enolase have been identified in the ESP. Enolase, observed to be one of the most abundant proteins, was further characterized. The molecular cloning and in vitro expression in Escherichia coli of E. caproni enolase allowed us to determine that the protein contains 431 amino acids and a theoretical MW of 46272 Da. E. caproni enolase shows high homology to other trematode enolases. The recombinant protein binds specifically to human plasminogen in vitr…

MaleImmunologyEnolaseBlotting WesternMolecular Sequence DataMolecular cloningBiologymedicine.disease_causeGene Expression Regulation Enzymologiclaw.inventionlawCricetinaeEchinostomamedicineAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularRats WistarEscherichia coliActinchemistry.chemical_classificationMesocricetusSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionPlasminogenGeneral MedicineMolecular biologyIn vitroRecombinant ProteinsAmino acidRatsInfectious DiseaseschemistryBiochemistryExcretory systemPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationRecombinant DNAParasitologyElectrophoresis Polyacrylamide GelSequence AlignmentExperimental parasitology
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Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion

1996

International audience; Friedreich's ataxia (FRDA) is an autosomal recessive, degenerative disease that involves the central and peripheral nervous systems and the heart. A gene, X25, was identified in the critical region for the FRDA locus on chromosome 9q13. This gene encodes a 210-amino acid protein, frataxin, that has homologs in distant species such as Caenorhabditis elegans and yeast. A few FRDA patients were found to have point mutations in X25, but the majority were homozygous for an unstable GAA trinucleotide expansion in the first X25 intron.

MaleIron-sulfur cluster assemblyPolymerase Chain Reaction0302 clinical medicineTrinucleotide RepeatsIron-Binding ProteinsGenetics0303 health sciencesMultidisciplinaryAutosomal recessive cerebellar ataxiaPedigree3. Good healthFemalemedicine.symptomChromosomes Human Pair 9HumanPair 9Heterozygotecongenital hereditary and neonatal diseases and abnormalitiesAtaxiaMolecular Sequence DataGenes RecessiveLocus (genetics)BiologyChromosomes03 medical and health sciencesGene mappingAlleles; Amino Acid Sequence; Base Sequence; Chromosomes Human Pair 9; DNA Primers; Female; Friedreich Ataxia; Genes Recessive; Heterozygote; Humans; Male; Molecular Sequence Data; Pedigree; Point Mutation; Polymerase Chain Reaction; Proteins; Sequence Alignment; Introns; Iron-Binding Proteins; Trinucleotide RepeatsmedicineRecessiveHumansPoint MutationAmino Acid SequenceAlleleAllelesDNA Primers030304 developmental biologyBase SequencePoint mutationProteins[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologymedicine.diseaseMolecular biologyIntronsGenes[SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human geneticsFriedreich AtaxiaFrataxinbiology.proteinSequence Alignment030217 neurology & neurosurgeryScience
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Evolution of chromatin-remodeling complexes: comparative genomics reveals the ancient origin of "novel" compensasome genes.

2003

Dosage compensation in Drosophila is mediated by a complex, called compensasome, com- posed of at least five proteins and two noncoding RNAs. Genes encoding compensasome proteins have been collectively named male-specific lethals or msls. Recent work showed that three of the Drosophila msls (msl-3, mof, and mle) have an ancient origin. In this study, I describe likely orthologues of the two re- maining msls, msl-1 and msl-2, in several inverte- brates and vertebrates. The MSL-2 protein is the only one found in Drosophila and vertebrate genomes that contains both a RING finger and a peculiar type of CXC domain, related to the one present in Enhancer of Zeste proteins. MSL-1 also contains two…

MaleLeucine zipperAmino Acid MotifsMolecular Sequence DataBiologyGenomeChromatin remodelingEvolution MolecularDosage Compensation GeneticGeneticsRing fingermedicineAnimalsDrosophila ProteinsHumansAmino Acid SequenceEnhancerMolecular BiologyEcology Evolution Behavior and SystematicsCaenorhabditis elegansPhylogenyComparative genomicsGeneticsDosage compensationfungiNuclear ProteinsGenomicsbiology.organism_classificationChromatin Assembly and DisassemblyProtein Structure TertiaryDNA-Binding Proteinsmedicine.anatomical_structureVertebratesDrosophilaSequence AlignmentTranscription FactorsJournal of molecular evolution
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