Search results for "Multigene"

showing 10 items of 145 documents

Identification of a positively evolving putative binding region with increased variability in posttranslational motifs in zonadhesin MAM domain 2.

2005

Positive selection has been shown to be pervasive in sex-related proteins of many metazoan taxa. However, we are only beginning to understand molecular evolutionary processes on the lineage to humans. To elucidate the evolution of proteins involved in human reproduction, we studied the sequence evolution of MAM domains of the sperm-ligand zonadhesin in respect to single amino acid sites, solvent accessibility, and posttranslational modification. GenBank-data were supplemented by new cDNA-sequences of a representative non-human primate panel. Solvent accessibility predictions identified a probably exposed fragment of 30 amino acids belonging to MAM domain 2 (i.e., MAM domain 3 in mouse). The…

GlycosylationGlycosylationMolecular Sequence DataBiologyProtein Serine-Threonine Kinaseschemistry.chemical_compoundMiceN-linked glycosylationGenetic variationGeneticsAnimalsAmino Acid SequenceBinding sitePhosphorylationSelection GeneticMolecular BiologyPeptide sequenceEcology Evolution Behavior and SystematicsBinding selectivitychemistry.chemical_classificationGeneticsBinding SitesBase SequenceSequence Homology Amino AcidGenetic VariationMembrane ProteinsAmino acidRepressor ProteinsSperm MaturationchemistryMultigene FamilyPhosphorylationProtein Processing Post-TranslationalTranscription FactorsMolecular phylogenetics and evolution
researchProduct

Membrane-insertion fragments of Bcl-xL, Bax, and Bid.

2004

Apoptosis regulators of the Bcl-2 family associate with intracellular membranes from mitochondria and the endoplasmic reticulum, where they perform their function. The activity of these proteins is related to the release of apoptogenic factors, sequestered in the mitochondria, to the cytoplasm, probably through the formation of ion and/or protein transport channels. Most of these proteins contain a C-terminal putative transmembrane (TM) fragment and a pair of hydrophobic alpha helices (alpha5-alpha6) similar to the membrane insertion fragments of the ion-channel domain of diphtheria toxin and colicins. Here, we report on the membrane-insertion properties of different segments from antiapopt…

GlycosylationStereochemistryRecombinant Fusion ProteinsMolecular Sequence Databcl-X ProteinBcl-xLApoptosisBiochemistryProtein Structure SecondaryMembrane LipidsMiceProtein structureBcl-2-associated X proteinPredictive Value of TestsProto-Oncogene ProteinsProtein Interaction MappingAnimalsHumansAmino Acid SequencePeptide sequencebcl-2-Associated X ProteinbiologyIntracellular MembranesTransmembrane proteinPeptide FragmentsTransport proteinProtein TransportProto-Oncogene Proteins c-bcl-2Multigene FamilyHelixbiology.proteinBiophysicsCarrier ProteinsHydrophobic and Hydrophilic InteractionsAlpha helixBH3 Interacting Domain Death Agonist ProteinBiochemistry
researchProduct

Artificial Chromosomes to Explore and to Exploit Biosynthetic Capabilities of Actinomycetes

2012

Actinomycetes are an important source of biologically active compounds, like antibiotics, antitumor agents, and immunosuppressors. Genome sequencing is revealing that this class of microorganisms has larger genomes relative to other bacteria and uses a considerable fraction of its coding capacity (5–10%) for the production of mostly cryptic secondary metabolites. To access actinomycetes biosynthetic capabilities or to improve the pharmacokinetic properties and production yields of these chemically complex compounds, genetic manipulation of the producer strains can be performed. Heterologous expression in amenable hosts can be useful to exploit and to explore the genetic potential of actinom…

Heterologous expression.DNA BacterialHealth Toxicology and Mutagenesislcsh:BiotechnologyHeterologouslcsh:MedicineHuman artificial chromosomeReview ArticleSettore BIO/19 - Microbiologia GeneraleStreptomycesGenomeMicrobial biotechnologyDNA sequencingSecondary metabolite03 medical and health scienceslcsh:TP248.13-248.65GeneticsChromosomes ArtificialMolecular BiologyGene030304 developmental biologyGene LibraryGenetics0303 health sciencesbiology030306 microbiologyActinomycetelcsh:RGeneral Medicinebiology.organism_classificationArtificial chromosomeBiosynthetic PathwaysActinobacteriaMultigene FamilyMolecular MedicineHeterologous expressionBacteriaBiotechnologyJournal of Biomedicine and Biotechnology
researchProduct

Evolutionary history of the OmpR/IIIA family of signal transduction two component systems in Lactobacillaceae and Leuconostocaceae

2011

15 pages, 3 tables, 7 figures.

Histidine KinaseEvolutionMolecular Sequence DataSignal transductionEvolution MolecularBacterial ProteinsPhylogeneticsQH359-425Lactic acid bacteriaAmino Acid SequenceGeneEcology Evolution Behavior and SystematicsPhylogenyGeneticsTwo component systemLeuconostocaceaebiologyPhylogenetic treeLactobacillalesfungiLactobacillaceaebiology.organism_classificationTwo-component regulatory systemResponse regulatorLactobacillaceaeMultigene FamilyLeuconostocaceaeProtein KinasesSequence AlignmentOmpR/IIIA familyResearch Article
researchProduct

Evolutionary conservation and function of the human embryonic stem cell specific miR-302/367 cluster

2015

miRNA clusters define a group of related miRNAs closely localized in the genome with an evolution that remains poorly understood. The miR-302/367 cluster represents a single polycistronic transcript that produces five precursor miRNAs. The cluster is highly expressed and essential for maintenance of human embryonic stem cells. We found the cluster to be highly conserved and present in most mammals. In primates, seed sequence and miRNA structure are conserved, but inter-precursor sequences are evolving. Insertions of new miRNAs, deletions of individual miRNAs, and a cluster duplication observed in different species suggest an actively evolving cluster. Core transcriptional machinery consisti…

Homeobox protein NANOGPhysiologyHuman Embryonic Stem CellsMolecular Sequence DataTarget analysisSequence alignmentStem cellsBiologyBiochemistryGenomeConserved sequenceEvolution MolecularNeoplasmsGene duplicationmicroRNABiomarkers TumorGeneticsAnimalsHumansMolecular BiologyGeneCancermiRNAGeneticsBase Sequenceta1184Functional genomicskantasolutMicroRNAsMultigene FamilySequence AlignmentFunctional genomics
researchProduct

Identification of New Genetic Clusters in Glioblastoma Multiforme: EGFR Status and ADD3 Losses Influence Prognosis

2020

Glioblastoma multiforme (GB) is one of the most aggressive tumors. Despite continuous efforts to improve its clinical management, there is still no strategy to avoid a rapid and fatal outcome. EGFR amplification is the most characteristic alteration of these tumors. Although effective therapy against it has not yet been found in GB, it may be central to classifying patients. We investigated somatic-copy number alterations (SCNA) by multiplex ligation-dependent probe amplification in a series of 137 GB, together with the detection of EGFRvIII and FISH analysis for EGFR amplification. Publicly available data from 604 patients were used as a validation cohort. We found statistical associations…

IDHMaleOncologymedicine.medical_specialtyDNA Copy Number VariationsEGFRSCNAsurvivalArticleText miningCDKN2AInternal medicineHumansMedicineMultiplexlcsh:QH301-705.5<i>IDH</i>Brain Neoplasmsbusiness.industryGene AmplificationglioblastomaGeneral MedicineMiddle AgedADD3Prognosismedicine.diseaseSurvival AnalysisErbB ReceptorsMSH6high throughout techniqueslcsh:Biology (General)ADD3Multigene FamilyCalmodulin-Binding ProteinsFemaleprecisionIdentification (biology)businessSignal TransductionGlioblastomaCells
researchProduct

Molecular evolution of the arthropod hemocyanin superfamily.

2001

Arthropod hemocyanins are members of a protein superfamily that also comprises the arthropod phenoloxidases (tyrosinases), crustacean pseudohemocyanins (cryptocyanins), and insect storage hexamerins. The evolution of these proteins was inferred by neighbor-joining, maximum-parsimony, and maximum-likelihood methods. Monte Carlo shuffling approaches provided evidence against a discernible relationship of the arthropod hemocyanin superfamily and molluscan hemocyanins or nonarthropodan tyrosinases. Within the arthropod hemocyanin superfamily, the phenoloxidase probably emerged early in the (eu-)arthropod stemline and thus form the most likely outgroup. The respiratory hemocyanins evolved from t…

InsectaTime Factorsmedia_common.quotation_subjectmedicine.medical_treatmentLineage (evolution)Sequence alignmentInsectMolecular evolutionGeneticsmedicineAnimalsMolecular clockMolecular BiologyArthropodsEcology Evolution Behavior and Systematicsmedia_commonbiologyHemocyaninbiology.organism_classificationCrustaceanBiological EvolutionEvolutionary biologyMolluscaMultigene FamilyHemocyaninsArthropodSequence AlignmentMolecular biology and evolution
researchProduct

Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro.

2004

Abstract The oxygen sensor fumarate nitrate reductase regu-lator (FNR) of Escherichia coli contains in the active (anaerobic)state a [4Fe–4S] 2þ cluster which is lost after exposure to O 2 .Inaerobically prepared apoFNR, or in FNR obtained by treatmentof [4Fe–4S] FNR with O 2 in vitro, intramolecular cysteinedisulfides are found, including the cysteine residues which serveas ligands for the Fe–S cluster. It is shown here that thereconstitution of [4Fe–4S] FNR from this form of aerobicapoFNR was preceded by a long lag phase when glutathione wasused as the reducing agent. Addition of E. coli glutaredoxins(Grx) 1, 2 or 3 decreased the lag phase greatly and stimulatedthe reconstitution rate slig…

Iron-Sulfur ProteinsTime FactorsReducing agentFNRGlutaredoxinBiophysicsBiologyReductaseSulfidesmedicine.disease_causeNitrate reductaseBiochemistryOxygen sensorchemistry.chemical_compoundStructural BiologyGlutaredoxinGeneticsmedicineEscherichia coliCysteineDisulfidesThioredoxinMolecular BiologyEscherichia coliGlutaredoxinsDisulfide reductaseEscherichia coli ProteinsProteinsCell BiologyGlutathioneGlutathioneOxygenBiochemistrychemistryMultigene FamilyThioredoxinOxidoreductasesCysteineTranscription FactorsFEBS letters
researchProduct

Unique Microbial Catabolic Pathway for the Human Core N-Glycan Constituent Fucosyl-α-1,6-N-Acetylglucosamine-Asparagine

2020

The survival of commensal bacteria in the human gut partially depends on their ability to metabolize host-derived molecules. The use of the glycosidic moiety of N-glycoproteins by bacteria has been reported, but the role of N-glycopeptides or glycoamino acids as the substrates for bacterial growth has not been evaluated. We have identified in Lactobacillus casei strain BL23 a gene cluster (alf-2) involved in the catabolism of the glycoamino acid fucosyl-α-1,6-N-GlcNAc-Asn (6′FN-Asn), a constituent of the core-fucosylated structures of mammalian N-glycoproteins. The cluster consists of the genes alfHC, encoding a major facilitator superfamily (MFS) permease and the α-l-fucosidase AlfC, and t…

Lactobacillus caseiGlycanMolecular Biology and Physiologyalpha-l-fucosidaseGlycosylasparaginaseMicrobiologiacore fucosylationGut floraMicrobiologydigestive systemFucosylated Nglycopeptideschemistry.chemical_compoundVirologyfucosylated N-glycopeptidesN-AcetylglucosamineHumansAsparagineSymbiosisFucosebiologyHost Microbial InteractionsChemistryProbioticsbiology.organism_classificationMajor facilitator superfamilyQR1-502LactobacilsglycosylasparaginaseCore fucosylationGastrointestinal TractMetabolic pathwayLacticaseibacillus caseiBiochemistryAlpha-L-fucosidaseMultigene Familybiology.proteinAsparagineLactobacillus caseiBacteriaMetabolic Networks and PathwaysResearch Article
researchProduct

Malic Enzyme and Malolactic Enzyme Pathways Are Functionally Linked but Independently Regulated in Lactobacillus casei BL23

2013

ABSTRACT Lactobacillus casei is the only lactic acid bacterium in which two pathways for l -malate degradation have been described: the malolactic enzyme (MLE) and the malic enzyme (ME) pathways. Whereas the ME pathway enables L. casei to grow on l -malate, MLE does not support growth. The mle gene cluster consists of three genes encoding MLE ( mleS ), the putative l -malate transporter MleT, and the putative regulator MleR. The mae gene cluster consists of four genes encoding ME ( maeE ), the putative transporter MaeP, and the two-component system MaeKR. Since both pathways compete for the same substrate, we sought to determine whether they are coordinately regulated and their role in l -m…

Lactobacillus caseiPhysiologyMalatesMalic enzymeBiologyApplied Microbiology and BiotechnologyMalate dehydrogenaseGene Knockout TechniquesMalate DehydrogenaseGene clusterLactic AcidGeneRegulation of gene expressionEcologyActivator (genetics)Gene Expression ProfilingfungiBiological TransportTransporterGene Expression Regulation Bacterialrespiratory systembiology.organism_classificationCarbonLacticaseibacillus caseiBiochemistryMultigene FamilyEnergy MetabolismMetabolic Networks and PathwaysFood ScienceBiotechnologyApplied and Environmental Microbiology
researchProduct