Search results for "Sequence Homology"

showing 10 items of 477 documents

Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the correspondi…

1997

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 4…

0106 biological sciencesDNA ComplementaryMolecular Sequence DataBiology4-Hydroxyphenylpyruvate Dioxygenase01 natural sciencesBiochemistry03 medical and health sciencesDioxygenaseComplementary DNA[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceCells CulturedComputingMilieux_MISCELLANEOUS030304 developmental biologyHomogentisate 12-dioxygenase0303 health sciencesBase SequenceSequence Homology Amino AcidMolecular massDioxygenase activityNucleic acid sequenceCell BiologyMolecular biologyDaucus carotaBiochemistryElectrophoresis Polyacrylamide Gel4-Hydroxyphenylpyruvate dioxygenaseResearch ArticleChromatography LiquidSubcellular Fractions010606 plant biology & botany
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Expression of xyloglucan endotransglucosylase/hydrolase (XTH) genes and XET activity in ethylene treated apple and tomato fruits.

2013

[EN] Xyloglucan endotransglucosylase/hydrolase (XTHs: EC 2.4.1.207 and/or EC 3.2.1.151), a xyloglucan modifying enzyme, has been proposed to have a role during tomato and apple fruit ripening by loosening the cell wall. Since the ripening of climacteric fruits is controlled by endogenous ethylene biosynthesis, we wanted to study whether XET activity was ethylene-regulated, and if so, which specific genes encoding ripening-regulated XTH genes were indeed ethylene-regulated. XET specific activity in tomato and apple fruits was significantly increased by the ethylene treatment, as compared with the control fruits, suggesting an increase in the XTH gene expression induced by ethylene. The 25 Sl…

0106 biological sciencesEthylenePhysiologyPlant ScienceBiologyTransglucosylation and xyloglucan01 natural sciencesCell wall03 medical and health scienceschemistry.chemical_compoundSolanum lycopersicumPlant Growth RegulatorsGene Expression Regulation PlantGene expressionBIOQUIMICA Y BIOLOGIA MOLECULARGenePhylogeny030304 developmental biology2. Zero hunger0303 health sciencesSequence Homology Amino AcidCell wallAgriculturaGlycosyltransferasesfood and beveragesRipeningSequence Analysis DNAXyloglucan endotransglucosylaseEthylenesFruit ripeningXyloglucanMalus domesticachemistryBiochemistryFruitMalusClimactericAgronomy and Crop Science010606 plant biology & botany
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Demosponge EST sequencing reveals a complex genetic toolkit of the simplest metazoans.

2010

Sponges (Porifera) are among the simplest living and the earliest branching metazoans. They hold a pivotal role for studying genome evolution of the entire metazoan branch, both as an outgroup to Eumetazoa and as the closest branching phylum to the common ancestor of all multicellular animals (Urmetazoa). In order to assess the transcription inventory of sponges, we sequenced expressed sequence tag libraries of two demosponge species, Suberites domuncula and Lubomirskia baicalensis, and systematically analyzed the assembled sponge transcripts against their homologs from complete proteomes of six well-characterized metazoans--Nematostella vectensis, Caenorhabditis elegans, Drosophila melanog…

0106 biological sciencesGenome evolutionanimal structuresMolecular Sequence Datacomparative genomicsBiologyLubomirskia baicalensis010603 evolutionary biology01 natural sciencesGenomeEvolution Molecular03 medical and health sciencesGeneticsAnimalsCiona intestinalisMolecular BiologyGeneEcology Evolution Behavior and SystematicsPhylogenyResearch Articles030304 developmental biologymetazoan evolution; comparative genomics; genome complexity; Suberites domuncula; Lubomirskia baicalensisComparative genomicsGeneticsExpressed Sequence Tags0303 health sciencesComparative Genomic HybridizationGenomegenome complexityBase SequenceSequence Homology Amino Acidmetazoan evolutionbiology.organism_classificationSuberites domunculaEumetazoaPoriferaSuberites domunculaGene Expression RegulationSuberitesSequence AlignmentSuberitesMolecular biology and evolution
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Ultrastructure of regions containing homologous loci in polytene chromosomes of Drosophila melanogaster and Drosophila subobscura.

1998

We have used a new approach involving in situ hybridisation and electron microscopy to establish ultrastructural homologies between polytene chromosome regions of Drosophila melanogaster and Drosophila subobscura. Twelve probes were chosen to cover all the chromosomal elements: the myospheroid gene, the collagen type IV gene, the collagen-like gene, the w26 homeobox gene, the beta3 tubulin gene, the kinesin heavy chain gene, the tryptophan hydrolase gene, the Hsp82, Hsp22-26 and Hsp23-28, Hsp68, Hsp70 genes and the beta unit of the F0-F1 ATPase gene. Most of these loci were previously undescribed in D. subobscura and imprecisely located in D. melanogaster. We have demonstrated here, by an u…

0106 biological sciencesIntegrinsHSP30 Heat-Shock ProteinsKinesinsMuscle ProteinsLocus (genetics)Genes InsectTryptophan Hydroxylase010603 evolutionary biology01 natural sciencesHomology (biology)Chromosomes03 medical and health sciencesTubulinSequence Homology Nucleic AcidGeneticsMelanogasterAnimalsDrosophila ProteinsHSP20 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsGeneGenetics (clinical)Heat-Shock Proteins030304 developmental biologyGenetics0303 health sciencesPolytene chromosomebiologyMembrane Proteinsbiology.organism_classificationDrosophila subobscuraChromosome BandingProton-Translocating ATPasesDrosophila melanogasterChromosomal regionCollagenDrosophila melanogasterDNA ProbesIntegrin alpha ChainsChromosoma
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Transcriptome and proteome analysis of Pinctada margaritifera calcifying mantle and shell: focus on biomineralization

2010

Abstract Background The shell of the pearl-producing bivalve Pinctada margaritifera is composed of an organic cell-free matrix that plays a key role in the dynamic process of biologically-controlled biomineralization. In order to increase genomic resources and identify shell matrix proteins implicated in biomineralization in P. margaritifera, high-throughput Expressed Sequence Tag (EST) pyrosequencing was undertaken on the calcifying mantle, combined with a proteomic analysis of the shell. Results We report the functional analysis of 276 738 sequences, leading to the constitution of an unprecedented catalog of 82 P. margaritifera biomineralization-related mantle protein sequences. Component…

0106 biological sciencesModels MolecularProteomicsProteome[SDV]Life Sciences [q-bio]Proteomics01 natural sciencesContig MappingMantle (mollusc)MargaritiferaIn Situ HybridizationGeneticsExpressed Sequence Tags0303 health sciencesMineralsbiologyPinctada margaritifera[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeBiotechnologyResearch Articlelcsh:QH426-470Sequence analysislcsh:BiotechnologyMolecular Sequence Data010603 evolutionary biology03 medical and health sciencesCalcification Physiologiclcsh:TP248.13-248.65[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]GeneticsAnimals[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequencePinctadaRNA Messenger[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/Biomaterials030304 developmental biologyBase SequenceSequence Homology Amino AcidGene Expression ProfilingAnimal StructuresMolecular Sequence AnnotationSequence Analysis DNAbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialslcsh:GeneticsGene Expression RegulationEvolutionary biologyPinctadaBiomineralization
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An STE12 gene identified in the mycorrhizal fungus Glomus intraradices restores infectivity of a hemibiotrophic plant pathogen

2009

International audience; * • Mechanisms of root penetration by arbuscular mycorrhizal (AM) fungi are unknown and investigations are hampered by the lack of transformation systems for these unculturable obligate biotrophs. Early steps of host infection by hemibiotrophic fungal phytopathogens, sharing common features with those of AM fungal colonization, depend on the transcription factor STE12. * • Using degenerated primers and rapid amplification of cDNA ends, we isolated the full-length cDNA of an STE12-like gene, GintSTE, from Glomus intraradices and profiled GintSTE expression by real-time and in situ RT-PCR. GintSTE activity and function were investigated by heterologous complementation …

0106 biological sciencesPhysiologyGLOMUS INTRARADICESGenes FungalMolecular Sequence DataMutantGerminationMYCORHIZES ARBUSCULAIRESSaccharomyces cerevisiaePlant SciencePlant Roots01 natural sciencesMicrobiologyFungal ProteinsGlomeromycota03 medical and health sciencesHOST PENETRATIONFungal StructuresGene Expression Regulation FungalMycorrhizaeSequence Homology Nucleic AcidMedicago truncatulaColletotrichumAmino Acid SequenceRNA MessengerTRANSCRIPTION FACTORMycorrhizaSTE12030304 developmental biologyPhaseolus0303 health sciencesFungal proteinbiologyMYCORRHIZAReverse Transcriptase Polymerase Chain ReactionColletotrichum lindemuthianumGene Expression Profilingfungifood and beveragesSpores Fungalbiology.organism_classificationMedicago truncatula[SDV.BV.PEP]Life Sciences [q-bio]/Vegetal Biology/Phytopathology and phytopharmacyColletotrichumMutationHEMIBIOTROPHIC PATHOGENSequence AlignmentGLOMEROMYCOTA010606 plant biology & botany
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Reticulon-like proteins in Arabidopsis thaliana: structural organization and ER localization

2007

International audience; Reticulons are proteins that have been found predominantly associated with the endoplasmic reticulum in yeast and mammalian cells. While their functions are still poorly understood, recent findings suggest that they participate in the shaping of the tubular endoplamic reticulum (ER). Although reticulon-like proteins have been identified in plants, very little is known about their cellular localization and functions. Here, we characterized the reticulon-like protein family of Arabidopsis thaliana. Three subfamilies can be distinguished on the basis of structural organization and sequence homology. We investigated the subcellular localization of two members of the larg…

0106 biological sciencesProtein familyMolecular Sequence DataBiophysicsArabidopsis[SDV.BC]Life Sciences [q-bio]/Cellular BiologyRTLNB01 natural sciencesBiochemistryPlant Epidermis03 medical and health sciencesProtein structureStructural BiologyArabidopsisGeneticsArabidopsis thalianaAmino Acid SequenceMolecular BiologyCellular localizationConserved SequencePhylogeny030304 developmental biology0303 health sciencesbiologySequence Homology Amino AcidArabidopsis ProteinsEndoplasmic reticulumENDOPLASMIC RETICULUMCHLOROPLASTARABIDOPSIS THALIANACell BiologySubcellular localizationbiology.organism_classificationRETICULONBiochemistryReticulonRETICULON-LIKE PROTEIN BSequence Alignment010606 plant biology & botany
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The skeletal proteome of the coral Acropora millepora: the evolution of calcification by co-option and domain shuffling.

2013

14 pages; International audience; In corals, biocalcification is a major function that may be drastically affected by ocean acidification (OA). Scleractinian corals grow by building up aragonitic exoskeletons that provide support and protection for soft tissues. Although this process has been extensively studied, the molecular basis of biocalcification is poorly understood. Notably lacking is a comprehensive catalog of the skeleton-occluded proteins-the skeletal organic matrix proteins (SOMPs) that are thought to regulate the mineral deposition. Using a combination of proteomics and transcriptomics, we report the first survey of such proteins in the staghorn coral Acropora millepora. The or…

0106 biological sciencesProteomeCoralMolecular Sequence Datacalcium carbonate skeletonProteomics010603 evolutionary biology01 natural sciencesMass SpectrometryCalcium CarbonateEvolution Molecular03 medical and health sciencesAcropora milleporaCalcification PhysiologicproteomicsPhylogeneticsAnthozoa[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionGeneticsAnimals14. Life underwaterAmino Acid Sequencescleractinian[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular BiologyEcology Evolution Behavior and SystematicsDiscoveriesPhylogeny030304 developmental biologyStaghorn coral0303 health sciencesbiologySequence Homology Amino AcidEcologyMolecular Sequence Annotationbiology.organism_classification[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsAnthozoabiomineralizationExtracellular MatrixProtein Structure TertiaryEvolutionary biology[ SDV.BBM.GTP ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]ProteomeSequence AlignmentFunction (biology)
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Regulation of reactive oxygen species production by a 14-3-3 protein in elicited tobacco cells.

2007

International audience; The regulation of the system responsible for the production of reactive oxygen species (ROS) during plant–microorganism interaction is still largely unknown. The protein NtrbohD has been recently demonstrated as the plasma membrane oxidase responsible for ROS production in elicited tobacco cells. Here, its C-terminus part was used as a bait in a two-hybrid screen in order to identify putative regulators of this system. This led to the isolation of a cDNA coding for a member of the 14-3-3 protein family. The corresponding transcript was induced after infiltration of tobacco leaves with the fungal elicitor cryptogein. Tobacco cells transformed with an antisense constru…

0106 biological sciencesSIGNALLINGDNA ComplementaryProtein familyPhysiologyMolecular Sequence DataContext (language use)Plant ScienceBiology01 natural sciences03 medical and health sciencesTwo-Hybrid System TechniquesTobaccoNADPH OXIDASEAmino Acid Sequence14-3-3 protein030304 developmental biologychemistry.chemical_classification[SDV.EE]Life Sciences [q-bio]/Ecology environment0303 health sciencesReactive oxygen speciesOxidase testCRYPTOGEINNADPH oxidaseSequence Homology Amino AcidElicitorchemistryBiochemistry14-3-3 ProteinsNAD(P)H oxidasebiology.proteinReactive Oxygen Species010606 plant biology & botanyPlant, cellenvironment
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An isoleucine-leucine substitution in chloroplastic acetyl-CoA carboxylase from green foxtail (Setaria viridis L. Beauv.) is responsible for resistan…

2002

The cDNAs encoding chloroplastic acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) from three lines of Setaria viridis (L. Beauv.) resistant or sensitive to sethoxydim, and from one sethoxydim-sensitive line of Setaria italica (L. Beauv.) were cloned and sequenced. Sequence comparison revealed that a single isoleucine-leucine substitution discriminated ACCases from sensitive and resistant lines. Using near-isogenic lines of S. italica derived from interspecific hybridisation, we demonstrated that the transfer of the S. viridis mutant ACCase allele into a sethoxydim-sensitive S. italica line conferred resistance to this herbicide. We confirmed this result using allele-specific polymerase chain rea…

0106 biological sciencesSetariaChloroplastsMutantMolecular Sequence DataDrug ResistancePlant ScienceMolecular cloningPoaceae01 natural sciences[SDV.GEN.GPL]Life Sciences [q-bio]/Genetics/Plants geneticsLeucine[SDV.GEN.GPL] Life Sciences [q-bio]/Genetics/Plants geneticsGeneticsPoint MutationAmino Acid SequenceIsoleucineComputingMilieux_MISCELLANEOUSAllelesPhylogenyGenes DominantbiologySequence Homology Amino AcidSetaria viridisCyclohexanonesHerbicidesAcetyl-CoA carboxylase04 agricultural and veterinary sciencesbiology.organism_classification3. Good healthPyruvate carboxylaseBiochemistryAmino Acid Substitution040103 agronomy & agriculture0401 agriculture forestry and fisheriesLeucineIsoleucineSequence Alignment010606 plant biology & botanyAcetyl-CoA CarboxylasePlanta
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