Search results for "Amino acid sequence"

showing 10 items of 1296 documents

Characterization and Expression of Multiple Alternatively Spliced Transcripts of the Goodpasture Antigen Gene Region. Goodpasture Antibodies Recogniz…

1995

Collagen IV, the major component of basement membranes, is composed of six distinct alpha chains (alpha 1-alpha 6). Atypically among the collagen IV genes, the exons encoding the carboxyl-terminal region of the human alpha 3(IV) chain undergo alternative splicing. This region has been designated as the Goodpasture antigen because of its reactivity in the kidney and lung with the pathogenic autoantibodies causing Goodpasture syndrome. The data presented in this report demonstrate that, in human kidney, the gene region encompassing the Goodpasture antigen generates at least six alternatively spliced transcripts predicting five distinct proteins that differ in their carboxyl-terminus and retai…

Collagen Type IVTranscription GeneticAnti-Glomerular Basement Membrane DiseaseMolecular Sequence DataGene ExpressionBiologyAutoantigensPolymerase Chain ReactionBiochemistrylaw.inventionMiceExonAntigenIn vivolawmedicineAnimalsHumansGoodpasture syndromeAmino Acid SequenceRNA MessengerGeneAutoantibodiesDNA PrimersMice Inbred BALB CBase SequenceAlternative splicingAutoantibodymedicine.diseaseMolecular biologyRecombinant ProteinsAlternative SplicingRecombinant DNAbiology.proteinCollagenAntibodyEuropean Journal of Biochemistry
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Copy number variation and missense mutations of the agouti signaling protein (ASIP) gene in goat breeds with different coat colors.

2009

In goats, classical genetic studies reported a large number of alleles at the Agouti locus with effects on coat color and pattern distribution. From these early studies, the dominant A(Wt) (white/tan) allele was suggested to cause the white color of the Saanen breed. Here, we sequenced the coding region of the goat ASIP gene in 6 goat breeds (Girgentana, Maltese, Derivata di Siria, Murciano-Granadina, Camosciata delle Alpi, and Saanen), with different coat colors and patterns. Five single nucleotide polymorphisms (SNPs) were identified, 3 of which caused missense mutations in conserved positions of the cysteine-rich carboxy-terminal domain of the protein (p.Ala96Gly, p.Cys126Gly, and p.Val1…

Comparative Genomic HybridizationBase SequenceDNA Copy Number VariationsGoatsCapra hircuCNVMolecular Sequence DataMutation MissenseSNPColorBreedingPolymorphism Single NucleotideCOAT COLORSettore AGR/17 - Zootecnica Generale E Miglioramento GeneticoBREEDSaCGHAgouti locuASIP GENEGOATAgouti Signaling ProteinAnimalsHumansAmino Acid SequenceSequence AlignmentCytogenetic and genome research
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Compression-based classification of biological sequences and structures via the Universal Similarity Metric: experimental assessment.

2007

Abstract Background Similarity of sequences is a key mathematical notion for Classification and Phylogenetic studies in Biology. It is currently primarily handled using alignments. However, the alignment methods seem inadequate for post-genomic studies since they do not scale well with data set size and they seem to be confined only to genomic and proteomic sequences. Therefore, alignment-free similarity measures are actively pursued. Among those, USM (Universal Similarity Metric) has gained prominence. It is based on the deep theory of Kolmogorov Complexity and universality is its most novel striking feature. Since it can only be approximated via data compression, USM is a methodology rath…

Computer scienceAlgorismesPrediction by partial matchingCompression dissimilaritycomputer.software_genreBiochemistryProtein Structure SecondaryPhylogenetic studiesStructural BiologySequence Analysis ProteinDatabases Proteinlcsh:QH301-705.5Biological dataNCDApplied MathematicsGenomicsClassificationCDComputer Science ApplicationsBenchmarking:Informàtica::Informàtica teòrica [Àrees temàtiques de la UPC]Universal compression dissimilarityArea Under CurveMetric (mathematics)lcsh:R858-859.7Data miningAlgorithmsData compressionResearch Article:Informàtica::Aplicacions de la informàtica::Bioinformàtica [Àrees temàtiques de la UPC]Normalization (statistics)lcsh:Computer applications to medicine. Medical informaticsBioinformatics Sequence Alignment AlgorithmsSet (abstract data type)Similarity (network science)Normalized compression sissimilarityData compression (Computer science)AnimalsHumansAmino Acid SequenceMolecular BiologyBiologyDades -- Compressió (Informàtica)USMUniversal similarity metricProteinsUCDProtein Structure TertiaryData setGenòmicaStatistical classificationlcsh:Biology (General)ROC CurvecomputerSequence AlignmentSoftwareBMC bioinformatics
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Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal alpha-toxin.

1996

Staphylococcus aureus alpha-toxin is a hydrophilic polypeptide of 293 amino acids that produces heptameric transmembrane pores. During assembly, the formation of a pre-pore precedes membrane permeabilization; the latter is linked to a conformational change in the oligomer. Here, 41 single-cysteine replacement toxin mutants were thiol-specifically labelled with the polarity-sensitive fluorescent probe acrylodan. After oligomerization on membranes, only the mutants with acrylodan attached to residues in the sequence 118-140 exhibited a marked blue shift in the fluorescence emission maximum, indicative of movement of the fluorophore to a hydrophobic environment. Within this region, two functio…

Conformational changeStaphylococcus aureusProtein ConformationMembrane lipidsBacterial ToxinsMolecular Sequence DataBiologyGeneral Biochemistry Genetics and Molecular BiologyCell membraneHemolysin ProteinsProtein structure2-NaphthylaminemedicinePoint MutationAmino Acid SequenceCysteineMolecular BiologyPeptide sequenceFluorescent Dyeschemistry.chemical_classificationBinding SitesGeneral Immunology and MicrobiologyMolecular StructureGeneral NeuroscienceCell MembraneTransmembrane proteinAmino acidmedicine.anatomical_structureMembraneSpectrometry FluorescenceBiochemistrychemistryLiposomesBiophysicsMutagenesis Site-DirectedResearch ArticleThe EMBO journal
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Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer.

2004

Summary In mammals and yeast, a cytosolic dilysine motif is critical for endoplasmic reticulum (ER) localization of type I membrane proteins. Retrograde transport of type I membrane proteins containing dilysine motifs at their cytoplasmic carboxy (C)-terminal tail involves the interaction of these motifs with the COPI coat. The C-terminal dilysine motif has also been shown to confer ER localization to type I membrane proteins in plant cells. Using in vitro binding assays, we have analyzed sorting motifs in the cytosolic tail of membrane proteins, which may be involved in the interaction with components of the COPI coat in plant cells. We show that a dilysine motif in the −3,−4 position (rel…

CooperativityPlant ScienceBiologyCoatomer Proteinchemistry.chemical_compoundGeneticsAmino Acid SequencePlant ProteinsBinding SitesSequence Homology Amino AcidEndoplasmic reticulumProtoplastsMembrane ProteinsOryzaCell BiologyEndoplasmic reticulum localizationCOPIBrefeldin APeptide FragmentsCell biologyKineticsProtein SubunitsMembrane proteinchemistryAmino Acid SubstitutionCoatomerCytoplasmADP-Ribosylation Factor 1Sequence AlignmentSignal TransductionThe Plant journal : for cell and molecular biology
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Strong Cooperativity and Loose Geometry between CUB Domains Are the Basis for Procollagen C-Proteinase Enhancer Activity

2009

Procollagen C-proteinase enhancers (PCPE-1 and -2) specifically activate bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family during C-terminal processing of fibrillar collagen precursors. PCPEs consist of two CUB domains (CUB1 and CUB2) and one NTR domain separated by one short and one long linker. It was previously shown that PCPEs can strongly interact with procollagen molecules, but the exact mechanism by which they enhance BMP-1 activity remains largely unknown. Here, we used a series of deletion mutants of PCPE-1 and two chimeric constructs with repetitions of the same CUB domain to study the role of each domain and linker. Out of all the forms teste…

CooperativityPlasma protein bindingTransfectionBinding CompetitiveBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1Cell LineHumansAmino Acid SequenceBinding siteEnhancerMolecular BiologyGlycoproteinsExtracellular Matrix ProteinsBinding SitesEnzyme Catalysis and RegulationChemistryCircular DichroismCell BiologyCUB domainKineticsProcollagen peptidaseBiochemistryMutationBiophysicsElectrophoresis Polyacrylamide GelLinkerProcollagenProtein BindingJournal of Biological Chemistry
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Zn(II)-alloferon complexes - Similar sequence, different coordination modes, no antibacterial activity.

2020

Often, in the search for a highly defined scientific phenomenon, a different one becomes apparent. This was also the case of this work, in the scope of which we planned to search for metal-enhanced, novel antibacterial/ antifungal compounds. Instead, we denied the existence of such and revealed the details of the bioinorganic chemistry of Zn(II)-alloferon complexes. Zinc(II) complexes of alloferon 1 and 2, ligands with a sequential difference of one amino acid only, show a substantially different coordination pattern at physiological pH. In the case of Zn(II)-alloferon 1 species, a histamine-like binding mode is observed (N-terminal amine and imidazole of His-1) and the coordination sphere …

Coordination sphereAlloferon; Metal-antimicrobial peptide complex; Metal-peptide thermodynamics; Zinc(II)StereochemistryProton Magnetic Resonance Spectroscopychemistry.chemical_elementZincMicrobial Sensitivity Tests010402 general chemistryLigands01 natural sciencesBiochemistryMass SpectrometryInorganic ChemistryAlloferonchemistry.chemical_compoundStructure-Activity RelationshipCoordination ComplexesImidazoleMetal-antimicrobial peptide complexHistidineAmino Acid Sequencechemistry.chemical_classificationMetal-peptide thermodynamics010405 organic chemistryBioinorganic chemistryZinc(II)0104 chemical sciencesAmino acidAnti-Bacterial AgentsZincchemistryThermodynamicsChemical stabilityAmine gas treatingAntibacterial activityPeptidesJournal of inorganic biochemistry
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Toll-like receptors are part of the innate immune defense system of sponges (demospongiae: Porifera).

2006

During evolution and with the emergence of multicellular animals, the need arose to ward off foreign organisms that threaten the integrity of the animal body. Among many different receptors that participate in the recognition of microbial invaders, toll-like receptors (TLRs) play an essential role in mediating the innate immune response. After binding distinct microbial components, TLRs activate intracellular signaling cascades that result in an induced expression of diverse antimicrobial molecules. Because sponges (phylum Porifera) are filter feeders, they are abundantly exposed to microorganisms that represent a potential threat. Here, we describe the identification, cloning, and deduced …

CroatiaMolecular Sequence Datachemistry.chemical_compoundGeneticsAnimalsCluster AnalysisAmino Acid SequenceReceptorMolecular BiologyEcology Evolution Behavior and SystematicsIn Situ HybridizationPhylogenyDeath domainDNA PrimersToll-like receptorInnate immune systembiologyBase SequenceEffectorToll-Like ReceptorsLipopeptideSequence Analysis DNAbiology.organism_classificationBlotting NorthernImmunohistochemistryImmunity InnateCell biologyPoriferaSuberites domunculaInterleukin-1 Receptor-Associated KinaseschemistryCaspasesImmunologySignal transductionMolecular biology and evolution
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Identification, sequence and mRNA expression pattern during metamorphosis of a cDNA encoding a glycine-rich cuticular protein in Tenebrio molitor

1995

The study of insect cuticular proteins and their sequences is of interest because they are involved in protein-protein and protein-chitin interactions which confer the mechanical properties and fine architecture of the cuticle. Moreover, in the coleopteran Tenebrio molitor there is a dramatic change in cuticular architecture between pre- and postecdysial secretion. We report the isolation, by differential screening, and the sequence characterization of a cDNA clone encoding a cuticular protein of T. molitor, ACP17. After insertion in the expression vector pEX1, the recognition of the fusion protein by an anti-cuticular monoclonal antibody confirmed the cuticular nature of ACP17. Northern hy…

CuticleMolecular Sequence DataGene ExpressionBiologyComplementary DNAGene expressionGeneticsProtein biosynthesisAnimalsTissue DistributionAmino Acid SequenceRNA MessengerTenebrioPeptide sequenceIn Situ Hybridizationchemistry.chemical_classificationExpression vectorBase SequenceMetamorphosis BiologicalProteinsSequence Analysis DNAGeneral MedicineMolecular biologyAmino acidchemistryProtein BiosynthesisEcdysisInsect ProteinsGene
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The Biosynthesis of Rare Homo-Amino Acid Containing Variants of Microcystin by a Benthic Cyanobacterium

2019

Microcystins are a family of chemically diverse hepatotoxins produced by distantly related cyanobacteria and are potent inhibitors of eukaryotic protein phosphatases 1 and 2A. Here we provide evidence for the biosynthesis of rare variants of microcystin that contain a selection of homo-amino acids by the benthic cyanobacterium Phormidium sp. LP904c. This strain produces at least 16 microcystin chemical variants many of which contain homophenylalanine or homotyrosine. We retrieved the complete 54.2 kb microcystin (mcy) gene cluster from a draft genome assembly. Analysis of the substrate specificity of McyB1 and McyC adenylation domain binding pockets revealed divergent substrate specificity …

CyanobacteriamassaspektrometriaMicrocystinstoksiinitPharmaceutical ScienceMicrocystinPlanktothrixcyanobacteriaArticlebiosynteesi03 medical and health scienceschemistry.chemical_compoundBiosynthesisBacterial ProteinsDrug DiscoveryGene clusterpolycyclic compoundspolyketide synthase (PKS)Protein Interaction Domains and MotifsAmino Acid SequenceAmino AcidssyanobakteeritPharmacology Toxicology and Pharmaceutics (miscellaneous)Genelcsh:QH301-705.5Phylogeny030304 developmental biologymass spectrometrychemistry.chemical_classification0303 health sciencesbiology030302 biochemistry & molecular biologyta1182Sequence Analysis DNAbiology.organism_classificationAmino acidEnzymechemistryBiochemistrylcsh:Biology (General)adenylation domainGenes BacterialMultigene Familynonribosomal peptide synthetase (NRPS)hepatotoxinMarine Drugs
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