Search results for "Escher"

showing 10 items of 728 documents

A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes

1999

The gene xynC encoding xylanase C from Bacillus sp. BP-23 was cloned and expressed in Escherichia coli. The nucleotide sequence of a 3538 bp DNA fragment containing xynC gene was determined, revealing an open reading frame of 3258 bp that encodes a protein of 120,567 Da. A comparison of the deduced amino acid sequence of xylanase C with known beta-glycanase sequences showed that the encoded enzyme is a modular protein containing three different domains. The central region of the enzyme is the catalytic domain, which shows high homology to family 10 xylanases. A domain homologous to family IX cellulose-binding domains is located in the C-terminal region of xylanase C, whilst the N-terminal r…

Molecular Sequence DataBacillusBiologymedicine.disease_causeMicrobiologyHomology (biology)Substrate Specificitychemistry.chemical_compoundCatalytic DomainEnzyme StabilityEscherichia colimedicineXylobioseAmino Acid SequenceCloning MolecularEscherichia coliPeptide sequencechemistry.chemical_classificationEndo-14-beta XylanasesSequence Homology Amino AcidThermophileTemperatureNucleic acid sequenceSequence Analysis DNAXylosidasesEnzymeBiochemistrychemistryGenes BacterialXylanaseSequence AlignmentMicrobiology
researchProduct

Crystallization and preliminary crystallographic study of a pheromone-binding protein from the cockroachLeucophaea maderae

2002

Pheromone-binding proteins (PBPs) are small helical proteins (13-18 kDa) present in various sensory organs of moths and other insect species. An antennal protein from the cockroach Leucophaea maderae (LmaPBP) has been found to share all the hallmarks of the PBP family and is expressed specifically in the female adult antennae, the gender that perceives the sex pheromone. Here, the crystallization of LmaPBP expressed as a recombinant protein in Escherichia coli periplasm is reported. Crystals of LmaPBP were obtained by the sitting-drop vapour-diffusion method using a nanodrop-dispensing robot. The protein crystallizes in two different crystal forms. Form 1 belongs to space group P1, with uni…

Molecular Sequence DataCockroachesCrystallography X-Raymedicine.disease_causelaw.inventionStructural Biologylawbiology.animalmedicineAnimalsAmino Acid SequenceCrystallizationEscherichia coliCockroachSequence Homology Amino AcidbiologyChemistryResolution (electron density)General MedicinePeriplasmic spaceRecombinant ProteinsCrystallographySex pheromoneRecombinant DNAInsect ProteinsFemaleCarrier ProteinsCrystallizationPheromone binding proteinSequence AlignmentActa Crystallographica Section D Biological Crystallography
researchProduct

Engineering a 2D protein-DNA crystal.

2005

(Figure Presented) Weaving with DNA: A DNA-binding protein was used to control the structure of a self-assembled 2D crystal. In the absence of protein, four oligonucleotides hybridize to form a Kagome lattice of interwoven double helices with p3 symmetry (see image). Addition of protein RuvA during assembly changes the symmetry and connectivity to give a DNA-protein crystal with an approximately square unit cell. © 2005 Wiley-VCH Verlag GmbH and Co. KGaA.

Molecular Sequence DataProtein dnaPlasma protein bindingCatalysislaw.inventionCrystalNucleic acid thermodynamicschemistry.chemical_compoundlawNanotechnologyBase sequenceCrystallizationOligonucleotide Array Sequence AnalysisDNA CruciformBase SequenceEscherichia coli ProteinsDNA HelicasesNucleic Acid HybridizationGeneral MedicineDNAGeneral ChemistryDNA-Binding ProteinsMicroscopy ElectronCrystallographychemistryBiochemistryCrystallizationDNAProtein BindingAngewandte Chemie (International ed. in English)
researchProduct

A Na+-coupled C4-dicarboxylate transporter (Asuc_0304) and aerobic growth of Actinobacillus succinogenes on C4-dicarboxylates

2014

Actinobacillus succinogenes, which is known to produce large amounts of succinate during fermentation of hexoses, was able to grow on C4-dicarboxylates such as fumarate under aerobic and anaerobic conditions. Anaerobic growth on fumarate was stimulated by glycerol and the major product was succinate, indicating the involvement of fumarate respiration similar to succinate production from glucose. The aerobic growth on C4-dicarboxylates and the transport proteins involved were studied. Fumarate was oxidized to acetate. The genome of A. succinogenes encodes six proteins with similarity to secondary C4-dicarboxylate transporters, including transporters of the Dcu (C4-dicarboxylate uptake), Dcu…

Molecular Sequence Datamedicine.disease_causeModels BiologicalMicrobiologyDivalentBacterial ProteinsFumaratesmedicineDicarboxylic AcidsAmino Acid SequenceAnaerobiosisCarbon RadioisotopesEscherichia coliPhylogenyDicarboxylic Acid Transporterschemistry.chemical_classificationbiologySodiumBiological TransportSuccinatesActinobacillusGene Expression Regulation BacterialFumarate reductasebiology.organism_classificationAerobiosisTransport proteinActinobacillus succinogenesGlucoseBiochemistrychemistrySymporterFermentationCotransporterSequence AlignmentMicrobiology
researchProduct

Evidence for Natural Horizontal Transfer of the pcpB Gene in the Evolution of Polychlorophenol-Degrading Sphingomonads

2002

ABSTRACT The chlorophenol degradation pathway in Sphingobium chlorophenolicum is initiated by the pcpB gene product, pentachlorophenol-4-monooxygenase. The distribution of the gene was studied in a phylogenetically diverse group of polychlorophenol-degrading bacteria isolated from contaminated groundwater in Kärkölä, Finland. All the sphingomonads isolated were shown to share pcpB gene homologs with 98.9 to 100% sequence identity. The gene product was expressed when the strains were induced by 2,3,4,6-tetrachlorophenol. A comparative analysis of the 16S rDNA and pcpB gene trees suggested that a recent horizontal transfer of the pcpB gene was involved in the evolution of the catabolic pat…

Molecular Sequence Datamedicine.disease_causeSphingomonasApplied Microbiology and BiotechnologyMixed Function OxygenasesGene product03 medical and health sciencesTransduction GeneticRNA Ribosomal 16SmedicineEnvironmental Microbiology and BiodegradationAmino Acid SequenceAlleleGeneEscherichia coli030304 developmental biologySphingobium chlorophenolicumGenetics0303 health sciencesSequence Homology Amino AcidEcologybiology030306 microbiologybiology.organism_classification16S ribosomal RNASphingomonasBiological EvolutionHorizontal gene transferChlorophenolsFood ScienceBiotechnologyApplied and Environmental Microbiology
researchProduct

Transmembrane signaling in the sensor kinase DcuS of Escherichia coli : A long-range piston-type displacement of transmembrane helix 2

2015

The C4-dicarboxylate sensor kinase DcuS is membrane integral because of the transmembrane (TM) helices TM1 and TM2. Fumarate-induced movement of the helices was probed in vivo by Cys accessibility scanning at the membrane-water interfaces after activation of DcuS by fumarate at the periplasmic binding site. TM1 was inserted with amino acid residues 21-41 in the membrane in both the fumarate-activated (ON) and inactive (OFF) states. In contrast, TM2 was inserted with residues 181-201 in the OFF state and residues 185-205 in the ON state. Replacement of Trp 185 by an Arg residue caused displacement of TM2 toward the outside of the membrane and a concomitant induction of the ON state. Results …

MultidisciplinaryChemistryEscherichia coli ProteinsCell MembranePeriplasmic spaceBiological SciencesLigand (biochemistry)medicine.disease_causeTransmembrane proteinCell membraneCrystallographyTransmembrane domainmedicine.anatomical_structureMembraneEscherichia colimedicineBiophysicsBinding siteProtein KinasesEscherichia coliSignal TransductionProceedings of the National Academy of Sciences
researchProduct

Major Histocompatibility Complex Class I Allele-specific Cooperative and Competitive Interactions between Immune Evasion Proteins of Cytomegalovirus

2002

Cytomegaloviruses (CMVs) deploy a set of genes for interference with antigen presentation in the major histocompatibility complex (MHC) class I pathway. In murine CMV (MCMV), three genes were identified so far: m04/gp34, m06/gp48, and m152/gp40. While their function as immunoevasins was originally defined after their selective expression, this may not necessarily reflect their biological role during infection. The three immunoevasins might act synergistically, but they might also compete for their common substrate, the MHC class I complexes. To approach this question in a systematic manner, we have generated a complete set of mutant viruses with deletions of the three genes in all seven pos…

Muromegalovirusmurine cytomegalovirusImmunologyAntigen presentationGenes MHC Class IMutagenesis (molecular biology technique)Context (language use)Virus ReplicationMajor histocompatibility complexPolymerase Chain ReactionArticleMiceViral ProteinsMuromegalovirusMHC class IEscherichia coliAnimalsImmunology and AllergyGeneAllelesBACimmune evasionGlycoproteinsGeneticsMice Inbred BALB CMembrane GlycoproteinsbiologyalleleFibroblastsbiology.organism_classificationViral replicationMHC class IIbiology.proteinCarrier ProteinsJournal of Experimental Medicine
researchProduct

Correlation between mutation rate and genome size in riboviruses: mutation rate of bacteriophage Qβ.

2013

Abstract Genome sizes and mutation rates covary across all domains of life. In unicellular organisms and DNA viruses, they show an inverse relationship known as Drake’s rule. However, it is still unclear whether a similar relationship exists between genome sizes and mutation rates in RNA genomes. Coronaviruses, the RNA viruses with the largest genomes (∼30 kb), encode a proofreading 3′ exonuclease that allows them to increase replication fidelity. However, it is unknown whether, conversely, the RNA viruses with the smallest genomes tend to show particularly high mutation rates. To test this, we measured the mutation rate of bacteriophage Qβ, a 4.2-kb levivirus. Amber reversion-based Luria–D…

Mutation rate[SDE.MCG]Environmental Sciences/Global ChangesMutantGenome ViralInvestigationsGenomeEvolution Molecular03 medical and health scienceschemistry.chemical_compound[SDV.EE.ECO]Life Sciences [q-bio]/Ecology environment/EcosystemsGenome SizeMutation Rate[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseasesGeneticsEscherichia coliGenome sizeComputingMilieux_MISCELLANEOUS030304 developmental biologyGenetics[SDV.EE.SANT]Life Sciences [q-bio]/Ecology environment/HealthAllolevivirus0303 health sciences[SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseasesbiology030302 biochemistry & molecular biologyRNAbiology.organism_classification[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology3. Good healthchemistry[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyProofreading[SDE.BE]Environmental Sciences/Biodiversity and EcologyBacteriophage QβDNAGenetics
researchProduct

Effect of mismatch repair on the mutation rate of bacteriophage ϕX174

2015

Viral mutation rates vary widely in nature, yet the mechanistic and evolutionary determinants of this variability remain unclear. Small DNA viruses mutate orders of magnitude faster than their hosts despite using host-encoded polymerases for replication, which suggests these viruses may avoid post-replicative repair. Supporting this, the genome of bacteriophage ϕX174 is completely devoid of GATC sequence motifs, which are required for methyl-directed mismatch repair in Escherichia coli . Here, we show that restoration of the randomly expected number of GATC sites leads to an eightfold reduction in the rate of spontaneous mutation of the phage, without severely impairing its replicative capa…

Mutation ratemutation rateBase analogBiologymedicine.disease_causeMicrobiologyGenomeBacteriophage03 medical and health scienceschemistry.chemical_compoundVirologyevolutionmedicinestress-induced mutagenesisEscherichia coli030304 developmental biologyGeneticsbacteriophage ϕX1740303 health sciencesmethyl-directed mismatch repair030302 biochemistry & molecular biologyMutagenesisbiology.organism_classificationchemistryDNA mismatch repairDNAResearch ArticleVirus Evolution
researchProduct

New insight into the haemoglobin superfamily: preliminary crystallographic characterization of human cytoglobin.

2003

Human cytoglobin, present in almost all tissue types, is a newly identified member of the Hb superfamily. A double mutant, having both cysteines replaced by serines, has been overexpressed in Escherichia coli, purified and crystallized. A highly redundant SAD data set has been collected at the haem Fe-atom absorption edge (lambda = 1.720 A) to 2.60 A resolution. The crystals belong to the orthorhombic P2(1)2(1)2(1) space group, with unit-cell parameters a = 46.8, b = 73.1, c = 98.9 A and two molecules per asymmetric unit. The anomalous difference Patterson map clearly reveals the position of the haem Fe-atom sites, thus paving the way for SAD structure determination.

MutationBinding SitesMolecular StructureIronCytoglobinResolution (electron density)CytoglobinMutation MissenseGeneral MedicineBiologyCrystallography X-Raymedicine.disease_causeGlobinsCrystallographyStructural BiologymedicineHumansMoleculeOrthorhombic crystal systemGlobinBinding siteCrystallizationEscherichia coli
researchProduct