Search results for "Conserved sequence"

showing 10 items of 103 documents

Similarities and singularities of three DnaK proteins from the cyanobacterium Synechocystis sp. PCC 6803.

2010

In the genome of completely sequenced mesophilic cyanobacterium Synechocystis sp. PCC 6803 three DnaK proteins are encoded, which share a high degree of sequence identity in their N-terminal ATPase region as well as in the adjacent peptide-binding domain. However, as typical for DnaK proteins, the C-termini of the three Synechocystis proteins are highly diverse. To study the functions of the three Synechocystis DnaK proteins in more detail, we have analyzed the abundance of the individual proteins in Synechocystis cells as well as dnaK expression under various stress conditions. The presented results show that all three Synechocystis DnaK proteins interact with the same GrpE nucleotide exch…

Physiologygenetic processesAmino Acid MotifsMolecular Sequence DataSequence alignmentPlant SciencePlasma protein bindingBiologymedicine.disease_causeMicrobiologyConserved sequenceNucleotide exchange factorBacterial ProteinsStress PhysiologicalmedicineHSP70 Heat-Shock ProteinsAmino Acid SequencePeptide sequenceConserved SequenceHeat-Shock ProteinsMutationSynechocystisSynechocystisCell BiologyGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationBiochemistrybiological sciencesMutationbacteriaSequence AlignmentFunction (biology)Protein BindingPlantcell physiology
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Evidence for an instructive role of apoptosis during the metamorphosis of Hydractinia echinata (Hydrozoa)

2011

Apoptosis is a highly conserved mechanism of cell deletion that destroys redundant, dysfunctional, damaged, and diseased cells. Furthermore, apoptotic cell death is essential during the development of multicellular organisms. However, there are only a few examples where the occurrence of apoptosis has been shown to be a direct prerequisite for developmental processes. As described previously by our group, the degradation of larval tissue during the first half of the metamorphosis of Hydractinia echinata involves extensive cell death. A large number of cells are removed, and we observed several cellular features of apoptotic cell death in the dying tissue, e.g., nucleosomal DNA fragmentation…

Programmed cell deathmedia_common.quotation_subjectMolecular Sequence DataCellApoptosisContext (language use)Gene Expression Regulation EnzymologicHydractinia echinatamedicineAnimalsAmino Acid SequenceMetamorphosisConserved SequencePhylogenyCaspasemedia_commonbiologyGene Expression ProfilingMetamorphosis Biologicalbiology.organism_classificationCell biologyHydrozoamedicine.anatomical_structureApoptosisCaspasesGene Knockdown Techniquesbiology.proteinDNA fragmentationAnimal Science and ZoologySequence AlignmentZoology
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Axolotl MHC architecture and polymorphism.

1999

The MHC of the urodele amphibian Ambystoma mexicanum consists of multiple polymorphic class I loci linked, so far as yet known, to a single class II B locus. This architecture is very different from that of the anuran amphibian Xenopus. The number of class I loci in the axolotl can vary from 6 to 21 according to the haplotypes as shown by cDNA analysis and Southern blot studies in families. These loci can be classified into seven sequence groups with features ranging from the class Ia to the class Ib type. All individuals express genes from at least three of the seven groups, and all individuals possess the class Ia-like type.

Protein ConformationImmunologyGenes MHC Class IIMolecular Sequence DataGenes MHC Class IMajor histocompatibility complexAmbystomaEvolution MolecularMajor Histocompatibility ComplexAxolotlPolymorphism (computer science)Complementary DNAHLA-A2 AntigenImmunology and AllergyAnimalsHumansAmino Acid SequenceAmbystoma mexicanumGeneConserved SequenceSouthern blotGeneticsPolymorphism GeneticbiologyHaplotypebiology.organism_classificationBlotting Southernbiology.proteinEuropean journal of immunology
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Crystal structure of bacteriophage fr capsids at 3.5 A resolution.

1994

The structure of recombinant capsids of the bacterial virus fr has been determined by X-ray crystallography at 3.5 A resolution. The capsids were produced by expressing the fr coat protein in Escherichia coli, the natural host of the virus, and are probably essentially identical to the protein shell of the native virus. The structure was determined using molecular replacement with the protein shell of the related MS2 virus, and refined to a crystallographic R-factor of 0.228. A comparison of the protein shells of the viruses shows that they are very similar, and indicates that they may have a similar regulation of the assembly of the quasi-symmetrical protein shell.

Protein ConformationvirusesMolecular Sequence DataRNA PhagesBiologymedicine.disease_causeCrystallography X-RayViruslaw.inventionBacteriophageCapsidStructural BiologylawmedicineComputer GraphicsEscherichia coliMolecular replacementAmino Acid SequenceMolecular BiologyEscherichia coliConserved SequenceLevivirusResolution (electron density)biology.organism_classificationRecombinant ProteinsCrystallographyCapsidMutationBiophysicsRecombinant DNABacterial virusSequence AlignmentJournal of molecular biology
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Phylointeractomics reconstructs functional evolution of protein binding

2017

Molecular phylogenomics investigates evolutionary relationships based on genomic data. However, despite genomic sequence conservation, changes in protein interactions can occur relatively rapidly and may cause strong functional diversification. To investigate such functional evolution, we here combine phylogenomics with interaction proteomics. We develop this concept by investigating the molecular evolution of the shelterin complex, which protects telomeres, across 16 vertebrate species from zebrafish to humans covering 450 million years of evolution. Our phylointeractomics screen discovers previously unknown telomere-associated proteins and reveals how homologous proteins undergo functiona…

Proteomics0301 basic medicineLineage (evolution)ScienceTelomere-Binding ProteinsGeneral Physics and AstronomyGenomicsBiologyProteomicsArticleGeneral Biochemistry Genetics and Molecular BiologyConserved sequenceEvolution Molecular03 medical and health sciencesPhylogeneticsMolecular evolutionPhylogenomicsAnimalsCells CulturedConserved SequencePhylogenyGeneticsGenomeMultidisciplinaryQComputational BiologyGenomicsSequence Analysis DNAGeneral ChemistryTelomereProtein superfamily030104 developmental biologyEvolutionary biologyVertebratesSequence AlignmentProtein Binding
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Identification of enolase as a plasminogen-binding protein in excretory-secretory products ofFasciola hepatica

2004

AbstractWe have followed a combined proteomic approach to identify proteins of Fasciola hepatica that could be involved in host–parasite interactions. Using two-dimensional gel electrophoresis, far Western immunoblot and mass spectrometry analyses, we have identified the enolase enzyme, present in the excretory/secretory materials of F. hepatica, as a human plasminogen-binding protein. This enzyme has an apparent molecular weight of 47 kDa with pI ranging from 6.2 to 7.2. These results suggest that enolase could act as a plasminogen receptor.

ProteomicsAmino Acid MotifsBlotting WesternMolecular Sequence DataEnolaseEnolaseBiophysicsProteomicsBiochemistryMass SpectrometryHost-Parasite InteractionsStructural BiologyHepaticaparasitic diseasesGeneticsAnimalsFasciola hepaticaElectrophoresis Gel Two-DimensionalAmino Acid SequenceIsoelectric PointPlasminogen bindingMolecular BiologyConserved Sequencechemistry.chemical_classificationGel electrophoresisSheepbiologyExcretory–secretoryPlasminogenHelminth ProteinsCell BiologyFasciola hepaticaHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyMolecular WeightBlotEnzymeLiverchemistryBiochemistryExcretory systemAntigens HelminthPhosphopyruvate HydrataseCarrier ProteinsFEBS Letters
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Tropomyosin: A panallergen that causes a worldwide allergic problem

2021

Background: Panallergens are proteins that take part in key processes of organisms and, therefore, are ubiquitously distributed with highly conserved sequences and structures. One class of these panallergens is composed of the tropomyosins. The highly heat-stable tropomyosins comprise the major allergens in crustaceans and mollusks, which make them important food allergens in exposed populations. Tropomyosins are responsible for a widespread immunoglobulin E cross-reactivity among allergens from different sources. Allergic tropomyosins are expressed in many species, including parasites and insects. Methods: This panallergen class is divided, according to it capacity of induced allergic symp…

Pulmonary and Respiratory Medicineinsect allergymacromolecular substancesCross Reactionsmedicine.disease_causeImmunoglobulin EConserved sequencetropomyosinAllergenFood allergybiology.animalmedicineImmunology and AllergyHumansAmino Acid Sequenceseafood allergyGeneticsfood allergybiologybusiness.industryVertebrateGeneral MedicineArticlesAllergensImmunoglobulin Emedicine.diseasemusculoskeletal systemTropomyosinIgE cross-reactivitypanallergenAllergic responsebiology.proteinhouse-dust mite allergyAllergistsbusinesstissuesFood Hypersensitivity
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Mapping and structure of DMXL1, a human homologue of the DmX gene from Drosophila melanogaster coding for a WD repeat protein.

2000

The DmX gene was recently isolated from the X chromosome of Drosophila melanogaster. TBLASTN searches of the dbEST databases revealed sequences with a high level of similarity to DmX in a variety of different species, including insects, nematodes, and mammals showing that DmX is an evolutionarily highly conserved gene. Here we describe the cloning of the cDNA and the chromosomal localization of one of the human homologues of DmX, Dmx-like 1 (DMXL1). The human DMXL1 gene codes for a large mRNA of 11 kb with an open reading frame of 3027 amino acids. The putative protein belongs to the superfamily of WD repeat proteins, which have mostly regulatory functions. The DMXL1 protein contains an exc…

Repetitive Sequences Amino AcidDNA ComplementaryMolecular Sequence DataBiologyConserved sequenceMiceGene mappingComplementary DNAGeneticsAnimalsDrosophila ProteinsHumansRadiation hybrid mappingAmino Acid SequenceDinucleotide RepeatsGeneIn Situ Hybridization FluorescenceGeneticsBase SequenceChromosome MappingProteinsbiology.organism_classificationOpen reading frameDrosophila melanogasterChromosomes Human Pair 5Insect ProteinsDrosophila melanogasterDrosophila ProteinGenomics
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REP2: A Web Server to Detect Common Tandem Repeats in Protein Sequences

2020

Ensembles of tandem repeats (TRs) in protein sequences expand rapidly to form domains well suited for interactions with proteins. For this reason, they are relatively frequent. Some TRs have known structures and therefore it is advantageous to predict their presence in a protein sequence. However, since most TRs diverge quickly, their detection by classical sequence comparison algorithms is not very accurate. Previously, we developed a method and a web server that used curated profiles and thresholds for the detection of 11 common TRs. Here we present a new web server (REP2) that allows the analysis of TRs in both individual and aligned sequences. We provide currently precomputed analyses f…

Repetitive Sequences Amino AcidWeb serverProteomeComputer scienceComputational biologycomputer.software_genreEvolution Molecular03 medical and health sciences0302 clinical medicineTandem repeatStructural BiologySequence comparisonHumansAmino Acid SequenceMolecular BiologyConserved Sequence030304 developmental biologySequence (medicine)Comparative genomicsInternet0303 health sciencesMultiple sequence alignmentBacteriaProteinsTandem Repeat SequencesProteomeUniProtSequence Alignmentcomputer030217 neurology & neurosurgeryJournal of Molecular Biology
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Evolutionary implications of intron-exon distribution and the properties and sequences of the RPL10A gene in eukaryotes.

2013

The RPL10A gene encodes the RPL10 protein, required for joining 40S and 60S subunits into a functional 80S ribosome. This highly conserved gene, ubiquitous across all eukaryotic super-groups, is characterized by a variable number of spliceosomal introns, present in most organisms. These properties facilitate the recognition of orthologs among distant taxa and thus comparative studies of sequences as well as the distribution and properties of introns in taxonomically distant groups of eukaryotes. The present study examined the multiple ways in which RPL10A conservation vs. sequence changes in the gene over the course of evolution, including in exons, introns, and the encoded proteins, can be…

Ribosomal ProteinsRibosomal Protein L10Molecular Sequence DataBiologyExon shufflingEvolution MolecularExonChlorophytaGeneticsMolecular BiologyGeneEcology Evolution Behavior and SystematicsConserved SequenceDNA PrimersGeneticsBase CompositionLikelihood FunctionsPhylogenetic treeBase SequenceModels GeneticIntronEukaryotaGenetic VariationBayes TheoremGroup II intronExonsSequence Analysis DNAIntronsEukaryotic RibosomeSequence AlignmentGC-contentMolecular phylogenetics and evolution
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