Search results for "Conserved sequence"

showing 10 items of 103 documents

Folding and stability of the aquaglyceroporin GlpF: Implications for human aqua(glycero)porin diseases

2015

AbstractAquaporins are highly selective polytopic transmembrane channel proteins that facilitate the permeation of water across cellular membranes in a large diversity of organisms. Defects in aquaporin function are associated with common diseases, such as nephrogenic diabetes insipidus, congenital cataract and certain types of cancer. In general, aquaporins have a highly conserved structure; from prokaryotes to humans. The conserved structure, together with structural dynamics and the structural framework for substrate selectivity is discussed. The folding pathway of aquaporins has been a topic of several studies in recent years. These studies revealed that a conserved protein structure ca…

Models MolecularProtein activityAmino Acid MotifsMolecular Sequence DataBiophysicsGene ExpressionPorinsAquaporinDiabetes Insipidus NephrogenicEndoplasmic-reticulum-associated protein degradationAquaporinsBiochemistryCataractProtein Structure SecondaryProtein structureNeoplasmsEscherichia coliGlpFHumansProtein foldingConserved SequenceProtein StabilityChemistryurogenital systemEscherichia coli ProteinsAquaporinWaterCell BiologyTransmembrane proteinCell biologyFolding (chemistry)Membrane proteinBiochemistryMembrane proteinPorinProtein foldingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
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The Structure of Rauvolfia serpentina Strictosidine Synthase Is a Novel Six-Bladed β-Propeller Fold in Plant Proteins

2006

Abstract The enzyme strictosidine synthase (STR1) from the Indian medicinal plant Rauvolfia serpentina is of primary importance for the biosynthetic pathway of the indole alkaloid ajmaline. Moreover, STR1 initiates all biosynthetic pathways leading to the entire monoterpenoid indole alkaloid family representing an enormous structural variety of ∼2000 compounds in higher plants. The crystal structures of STR1 in complex with its natural substrates tryptamine and secologanin provide structural understanding of the observed substrate preference and identify residues lining the active site surface that contact the substrates. STR1 catalyzes a Pictet-Spengler–type reaction and represents a novel…

Models MolecularTryptamineProtein FoldingStrictosidine synthaseProtein ConformationMolecular Sequence DataSequence alignmentPlant ScienceCatalysisRauwolfiaSubstrate Specificitychemistry.chemical_compoundRauvolfia serpentinaCarbon-Nitrogen LyasesAmino Acid SequenceResearch ArticlesConserved SequencePlant ProteinsBinding SitesSequence Homology Amino AcidbiologyIndole alkaloidActive siteCell BiologyLyasebiology.organism_classificationTryptamineschemistryBiochemistrybiology.proteinSecologaninSequence AlignmentThe Plant Cell
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Two α subunits and one β subunit of meprin zinc-endopeptidases are differentially expressed in the zebrafish Danio rerio

2007

Abstract Meprins are members of the astacin family of metalloproteases expressed in epithelial tissues, intestinal leukocytes and certain cancer cells. In mammals, there are two homologous subunits, which form complex glycosylated disulfide-bonded homo- and heterooligomers. Both human meprin α and meprin β cleave several basement membrane components, suggesting a role in epithelial differentiation and cell migration. There is also evidence that meprin β is involved in immune defence owing to its capability of activating interleukin-1β and the diminished mobility of intestinal leukocytes in meprin β-knockout mice. Here we show for the first time by reverse transcription PCR, immunoblotting a…

Molecular Sequence DataClinical BiochemistryDanioBiochemistryCatalysisChromosomesConserved sequenceAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyPeptide sequenceZebrafishConserved SequencePhylogenyZebrafishRegulation of gene expressionMessenger RNAbiologyMetalloendopeptidasesbiology.organism_classificationMolecular biologyProtein Structure TertiaryCell biologyProtein SubunitsZincGene Expression RegulationMicroscopy FluorescenceStructural Homology Proteinbiology.proteinAstacinSequence AlignmentATP synthase alpha/beta subunitsbchm
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A Globin Gene of Ancient Evolutionary Origin in Lower Vertebrates: Evidence for Two Distinct Globin Families in Animals

2004

Hemoglobin, myoglobin, neuroglobin, and cytoglobin are four types of vertebrate globins with distinct tissue distributions and functions. Here, we report the identification of a fifth and novel globin gene from fish and amphibians, which has apparently been lost in the evolution of higher vertebrates (Amniota). Because its function is presently unknown, we tentatively call it globin X (GbX). Globin X sequences were obtained from three fish species, the zebrafish Danio rerio, the goldfish Carassius auratus, and the pufferfish Tetraodon nigroviridis, and the clawed frog Silurana tropicalis. Globin X sequences are distinct from vertebrate hemoglobins, myoglobins, neuroglobins, and cytoglobins.…

Molecular Sequence DataConserved sequenceEvolution Molecularhemic and lymphatic diseasesbiology.animalGeneticsAnimalsAmino Acid SequenceRNA MessengerGlobinMolecular BiologyConserved SequencePhylogenyEcology Evolution Behavior and SystematicsSiluranaGeneticsSequence Homology Amino AcidbiologyCytoglobinFishesIntronVertebratebiology.organism_classificationGlobinsGlobin foldNeuroglobinAnuraProtein BindingMolecular Biology and Evolution
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Conserved Structure and Promoter Sequence Similarity in the Mouse and Human Genes Encoding the Zinc Finger Factor BERF-1/BFCOL1/ZBP-89

2001

Abstract We have characterized the genomic structure of the mouse Zfp148 gene encoding Beta-Enolase Repressor Factor-1 (BERF-1), a Kruppel-like zinc finger protein involved in the transcriptional regulation of several genes, which is also termed ZBP-89, BFCOL1. The cloned Zfp148 gene spans 110 kb of genomic DNA encompassing the 5′-end region, 9 exons, 8 introns, and the 3′-untranslated region. The promoter region displays the typical features of a housekeeping gene: a high G+C content and the absence of canonical TATA and CAAT boxes consistent with the multiple transcription initiation sites determined by primary extension analysis. Computer-assisted search in the human genome database allo…

Molecular Sequence DataResponse elementBiophysicsCodon InitiatorRegulatory Sequences Nucleic AcidBiologyBiochemistryConserved non-coding sequenceMiceExonAnimalsHumansPromoter Regions GeneticMolecular BiologyGeneConserved SequenceGeneticsZinc fingerBase SequenceAlternative splicingIntronZinc FingersPromoterExonsCell BiologyIntronsDNA-Binding ProteinsAlternative Splicing5' Untranslated RegionsTranscription FactorsBiochemical and Biophysical Research Communications
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The hemoglobin genes of Drosophila

2006

We recently reported the unprecedented occurrence of a hemoglobin gene (glob1) in the fruitfly Drosophila melanogaster. Here we investigate the structure and evolution of the glob1 gene in other Drosophila species. We cloned and sequenced glob1 genes and cDNA from D. pseudoobscura and D. virilis, and identified the glob1 gene sequences of D. simulans, D. yakuba, D. erecta, D. ananassae, D. mojavensis and D. grimshawi in the databases. Gene structure (introns in helix positions D7.0 and G7.0), gene synteny and sequence of glob1 are highly conserved, with high ds/dn ratios indicating strong purifying selection. The data suggest an important role of the glob1 protein in Drosophila, which may b…

Molecular Sequence DataSequence alignmentBiologyBiochemistryConserved sequenceEvolution MolecularHemoglobinsDrosophilidaeAnimalsDrosophila ProteinsGuanine Nucleotide Exchange FactorsAmino Acid SequenceGlobinCloning MolecularMolecular BiologyGeneConserved SequencePhylogenySyntenyGeneticsSequence Homology Amino AcidfungiIntronCell Biologybiology.organism_classificationDrosophilaDrosophila melanogasterSequence AlignmentFEBS Journal
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Comparative genomic sequencing reveals a strikingly similar architecture of a conserved syntenic region on human chromosome 11p15.3 (including gene S…

2001

Comparative genomics is a superior way to identify phylogenetically conserved features like genes or regions involved in gene regulation. The comparison of extended orthologous chromosomal regions should also reveal other characteristic traits essential for chromosome or gene function. In the present study we have sequenced and compared a region of conserved synteny from human chromosome 11p15.3 and mouse chromosome 7. In human, this region is known to contain several genes involved in the development of various disorders like Beckwith-Wiedemann overgrowth syndrome and other tumor diseases. Furthermore, in the neighboring chromosome region 11p15.5 extensive imprinting of genes has been repo…

Molecular Sequence DataeducationGenomicsBiologyChromosomesContig MappingMiceGene OrderGeneticsAnimalsHumansCloning MolecularMolecular BiologyGeneConserved SequenceGenetics (clinical)Repetitive Sequences Nucleic AcidSyntenyRegulation of gene expressionChromosome 7 (human)Comparative genomicsGeneticsChromosomes Human Pair 11Tumor Suppressor ProteinsGenomic sequencingChromosomeSequence Analysis DNAGC Rich SequenceDNA-Binding ProteinsCytogenetic and Genome Research
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Discovery and molecular characterization of a plasmid localized in Buchnera sp. bacterial endosymbiont of the aphid Rhopalosiphum padi

1995

We have identified and completely sequenced a novel plasmid isolated from the aphid Rhopalosiphum padi. Evidence which suggests that the plasmid occurs localized within the bacterial endosymbionts is presented. The plasmid contains the four genes that constitute the entire leucine operon. This fact makes it really unique since most plasmids are dispensable and lack genes that encode essential anabolic functions. Four more phloem-feeding aphid species also seem to contain homologous plasmids. Although further work is necessary, we hypothesize that this plasmid has appeared during the evolution of the symbiotic association between the aphid and the bacterial endosymbiont. The fact that this p…

OperonMolecular Sequence DataPlasmidSpecies SpecificityRhopalosiphum padiGram-Negative BacteriaGeneticsAnimalsAmino Acid SequenceSymbiosisMolecular BiologyGeneConserved SequenceEcology Evolution Behavior and SystematicsGeneticsAphidBase SequenceSequence Homology Amino AcidbiologyEndosymbiosisfungifood and beveragesbiochemical phenomena metabolism and nutritionbiology.organism_classificationAphidsRepliconDNA CircularLeucineBuchneraPlasmidsJournal of Molecular Evolution
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Modification of the proteolytic fragmentation pattern upon oxidation of cysteines from ribulose 1,5-bisphosphate carboxylase/oxygenase.

2003

The proteolytic susceptibility of the native CO 2 -fixing photosynthetic enzyme ribulose 1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39, Rubisco) has been shown to increase in vitro after oxidative treatments that affect cysteine thiols. A limited incubation of oxidized (pretreated with the disulfide cystamine) Rubisco from Chlamydomonas reinhardtii with subtilisin or proteinase K generated fragments of molecular mass about 53 kDa (band I in SDS-PAGE) and 47 kDa (band II) derived from the large subunit (55 kDa) of the enzyme. In contrast, proteolysis of the reduced Rubisco (pretreated with the free thiol cysteamine) produced only the 53 kDa band. The same fragmentation pattern was repr…

OxygenaseProtein subunitRibulose-Bisphosphate CarboxylaseMolecular Sequence DataBiochemistrychemistry.chemical_compoundEndopeptidasesAnimalsEuglena gracilisAmino Acid SequenceCysteineConserved SequenceRibulose 15-bisphosphatebiologyRibuloseHydrolysisfungiRuBisCOSubtilisinPeptide FragmentsKineticsProtein SubunitschemistryBiochemistryModels Chemicalbiology.proteinProtein quaternary structureHoloenzymesOxidation-ReductionProtein Processing Post-TranslationalChlamydomonas reinhardtiiCysteineBiochemistry
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