Search results for "alignment"

showing 10 items of 627 documents

Structural insights into the GTPase domain of Escherichia coli MnmE protein

2007

The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well…

Models MolecularTRNA modificationMagnetic Resonance SpectroscopyGTP'aluminium fluoridehomology modelingMolecular Sequence DataGTPaseGuanosine triphosphateGuanosine DiphosphateBiochemistryeraGTP Phosphohydrolaseschemistry.chemical_compoundStructural BiologyEscherichia coliAmino Acid SequenceHomology modelingBinding siteGTPaseMolecular BiologyBinding SitesSequence Homology Amino AcidChemistryEscherichia coli ProteinsTrmENMRRecombinant ProteinsKineticsBiochemistryMnmEGuanosine diphosphateRap2AGTP PhosphohydrolasesGuanosine TriphosphateSequence AlignmentRasProteins: Structure, Function, and Bioinformatics
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Characterisation, analysis of expression and localisation of the opsin gene repertoire from the perspective of photoperiodism in the aphid Acyrthosip…

2017

Organisms exhibit a wide range of seasonal responses as adaptions to predictable annual changes in their environment. These changes are originally caused by the effect of the Earth's cycles around the sun and its axial tilt. Examples of seasonal responses include floration, migration, reproduction and diapause. In temperate climate zones, the most robust variable to predict seasons is the length of the day (i.e. the photoperiod). The first step to trigger photoperiodic driven responses involves measuring the duration of the light-dark phases, but the molecular clockwork performing this task is poorly characterized. Photopigments such as opsins are known to participate in light perception, b…

Central Nervous SystemNymph0301 basic medicineOpsinPhysiologyPhotoperiodGene ExpressionDiapauseBiologyPolymerase Chain Reaction03 medical and health sciences0302 clinical medicineAnimalsPhotopigmentAmino Acid SequencePhylogenyphotoperiodismAphidOpsinsGene Expression Profilingfood and beveragesAphididaebiology.organism_classificationHemipteraAcyrthosiphon pisum030104 developmental biologyEvolutionary biologyAphidsInsect ScienceInsect ProteinsFemalePhotoreceptor Cells InvertebrateSequence Alignment030217 neurology & neurosurgeryJournal of Insect Physiology
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Usher syndrome and Leber congenital amaurosis are molecularly linked via a novel isoform of the centrosomal ninein-like protein.

2009

Contains fulltext : 80984.pdf (Publisher’s version ) (Closed access) Usher syndrome (USH) and Leber congenital amaurosis (LCA) are autosomal recessive disorders resulting in syndromic and non-syndromic forms of blindness. In order to gain insight into the pathogenic mechanisms underlying retinal degeneration, we searched for interacting proteins of USH2A isoform B (USH2A(isoB)) and the LCA5-encoded protein lebercilin. We identified a novel isoform of the centrosomal ninein-like protein, hereby named Nlp isoform B (Nlp(isoB)), as a common interactor. Although we identified the capacity of this protein to bind calcium with one of its three EF-hand domains, the interacton with USH2A(isoB) did …

Gene isoformRetinal degenerationCandidate geneGenetics and epigenetic pathways of disease [NCMLS 6]Usher syndromeMolecular Sequence DataOptic Atrophy Hereditary LeberBiologyIn Vitro TechniquesNeuroinformatics [DCN 3]CiliopathiesRetinaCell LineMiceCiliogenesisTwo-Hybrid System TechniquesGeneticsmedicineotorhinolaryngologic diseasesAnimalsHumansProtein IsoformsPhotoreceptor CellsAmino Acid SequenceNuclear proteinRats WistarEye ProteinsMolecular BiologyGenetics (clinical)GeneticsExtracellular Matrix ProteinsCiliumNuclear ProteinsGeneral MedicineArticlesmedicine.diseaseRatsMice Inbred C57BLMicrotubule-Associated ProteinsSequence AlignmentUsher SyndromesFunctional Neurogenomics [DCN 2]Protein BindingHuman Molecular Genetics
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Cloning and sequencing of the dnaK region of Streptomyces coelicolor A3(2)

1993

Abstract The dnaK homologue of Streptomyces coelicolor A3(2) strain M145 has been cloned and sequenced. Nucleotide sequence analysis of a 2.5-kb region revealed an open reading frame (ORF) encoding a predicted DnaK protein of 618 amino acids (Mr = 66 274). The dnaK coding sequence displays extreme codon bias and shows a strong preference for CGY and GGY, for Arg and Gly codons, respectively. The predicted DnaK sequence has a high Lys:Arg ratio which is not typical of streptomycete proteins. The region immediately downstream from dnaK contains an ORF for a GrpE-like protein; the predicted start codon of grpE overlaps the last two codons of dnaK, indicating that the two genes are translationa…

DNA BacterialMolecular Sequence Datagenetic processesBacterial ProteinsStart codonGeneticsCoding regionHSP70 Heat-Shock ProteinsAmino Acid SequenceCloning MolecularCodonGeneHeat-Shock Proteinschemistry.chemical_classificationGeneticsBase SequencebiologyEscherichia coli ProteinsStreptomyces coelicolorNucleic acid sequenceStreptococcusGeneral Medicinebiology.organism_classificationAmino acidOpen reading framechemistryGenes BacterialProtein BiosynthesisCodon usage biasbiological sciencesbacteriaSequence AlignmentGene
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Genes and derived amino acid sequences of S-layer proteins from mesophilic, thermophilic, and extremely thermophilic methanococci

2002

Cells of methanococci are covered by a single layer of protein subunits (S-layer) in hexagonal arrangement, which are directly exposed to the environment and which cannot be stabilized by cellular components. We have isolated S-layer proteins from cells of Methanococcus vannielii ( T(opt.)=37 degrees C), Methanococcus thermolithotrophicus ( T(opt.)=65 degrees C), and Methanococcus jannaschii ( T(opt.)=85 degrees C). The primary structure of the S-layer proteins was determined by sequencing the corresponding genes. According to the predicted amino acid sequence, the molecular masses of the S-layer proteins of the different methanococci are in a small range between 59,064 and 60,547 Da. Compa…

MethanococcusArchaeal ProteinsMethanococcusMolecular Sequence DataMicrobiologySpecies SpecificityMethanococcalesAmino Acid SequencePeptide sequencechemistry.chemical_classificationSequence Homology Amino AcidbiologyThermophileTemperatureProtein primary structureGeneral Medicinebiology.organism_classificationMethanococciAmino acidchemistryBiochemistryGenes BacterialMolecular MedicineSequence AlignmentS-layerBacterial Outer Membrane ProteinsExtremophiles
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A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model

2014

Chaperonins mediate protein folding in a cavity formed by multisubunit rings. The human CCT has eight non-identical subunits and the His147Arg mutation in one subunit, CCT5, causes neuropathy. Knowledge is scarce on the impact of this and other mutations upon the chaperone's structure and functions. To make progress, experimental models must be developed. We used an archaeal mutant homolog and demonstrated that the His147Arg mutant has impaired oligomeric assembly, ATPase activity, and defective protein homeostasis functions. These results establish for the first time that a human chaperonin gene defect can be reproduced and studied at the molecular level with an archaeal homolog. The major…

Models MolecularProtein FoldingProtein ConformationProtein subunitMutantMolecular Sequence Datahuman CCT5 gene mutation molecular dynamics neuropathy archaeal modelSequence alignmentGene mutationBiologyArticleChaperonin03 medical and health sciences0302 clinical medicineProtein structureHumansProtein Interaction Domains and MotifsAmino Acid Sequence030304 developmental biologyGenetics0303 health sciencesMultidisciplinarySettore BIO/16 - Anatomia UmanaArchaeaSettore CHIM/08 - Chimica FarmaceuticaChaperone (protein)Mutationbiology.proteinThermodynamicsProtein foldingProtein MultimerizationSequence Alignment030217 neurology & neurosurgeryChaperonin Containing TCP-1
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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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kmcEx: memory-frugal and retrieval-efficient encoding of counted k-mers.

2018

Abstract Motivation K-mers along with their frequency have served as an elementary building block for error correction, repeat detection, multiple sequence alignment, genome assembly, etc., attracting intensive studies in k-mer counting. However, the output of k-mer counters itself is large; very often, it is too large to fit into main memory, leading to highly narrowed usability. Results We introduce a novel idea of encoding k-mers as well as their frequency, achieving good memory saving and retrieval efficiency. Specifically, we propose a Bloom filter-like data structure to encode counted k-mers by coupled-bit arrays—one for k-mer representation and the other for frequency encoding. Exper…

Statistics and ProbabilitySource codeComputer sciencemedia_common.quotation_subject0206 medical engineeringHash function02 engineering and technologyBiochemistry03 medical and health sciencesEncoding (memory)Molecular BiologyTime complexity030304 developmental biologyBlock (data storage)media_common0303 health sciencesSequence Analysis DNAData structureComputer Science ApplicationsComputational MathematicsComputational Theory and MathematicsError detection and correctionAlgorithmSequence Alignment020602 bioinformaticsAlgorithmsSoftwareBioinformatics (Oxford, England)
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A new species of Pythium with filamentous sporangia having pectinolytic activities, isolated in the Burgundy region of France.

2001

A new species, Pythium pectinolyticum (F-83.1), isolated from soil samples taken in the Burgundy region is being described here. This species is characterised by its filamentous non-inflated type of sporangia, smooth-walled mostly catenulate oogonia and very rare antheridia. This fungus is a very slow-growing organism on most of the solid media, but it grows well in liquid media and also on those containing pectin as the sole source of carbon. Morphological features are described here together with the sequences of the internal transcribed spacer 1 region of the nuclear ribosomal DNA of the fungus, its comparison with related species, and its pectinolytic behaviour.

Molecular Sequence DataPythiumFungusMicrobiologyBotanyDNA Ribosomal SpacerGeneticsmedicinePythiumInternal transcribed spacerDNA FungalMolecular BiologyRibosomal DNASoil MicrobiologybiologyOogoniumBase SequenceSporangiumSequence Analysis DNAbiology.organism_classificationmedicine.anatomical_structureRNA RibosomalAntheridiumOosporePectinsFranceSequence AlignmentFEMS microbiology letters
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Amino acids in the second transmembrane helix of the Lhca4 subunit are important for formation of stable heterodimeric light-harvesting complex LHCI-…

2007

Photosynthetic light-harvesting complexes (LHCs) are assembled from apoproteins (Lhc proteins) and non-covalently attached pigments. Despite a considerable amino acid sequence identity, these proteins differ in their oligomerization behavior. To identify the amino acid residues determining the heterodimerization of Lhca1 and Lhca4 to form LHCI-730, we mutated the poorly conserved second transmembrane helix of the two subunits. Mutated genes were expressed in Escherichia coli and the resultant proteins were refolded in vitro and subsequently analyzed by gel electrophoresis. Replacement of the entire second helix in Lhca4 by the one of Lhca3 abolished heterodimerization, whereas it had no eff…

ChlorophyllModels MolecularMolecular Sequence DataLight-Harvesting Protein ComplexesBiologyProtein Structure SecondarySerineSolanum lycopersicumStructural BiologyChlorophyll bindingConsensus sequenceHistidineHomology modelingAmino Acid SequenceAmino AcidsProtein Structure QuaternaryMolecular BiologyPeptide sequenceHistidinePlant Proteinschemistry.chemical_classificationPhotosystem I Protein ComplexAmino acidTransmembrane domainProtein SubunitschemistryBiochemistryMutagenesisChlorophyll Binding ProteinsDimerizationSequence AlignmentJournal of molecular biology
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