0000000000594460

AUTHOR

Lorenzo Durante

showing 2 related works from this author

Complete sequencing of Novosphingobium sp. PP1Y reveals a biotechnologically meaningful metabolic pattern.

2014

Background Novosphingobium sp. strain PP1Y is a marine α-proteobacterium adapted to grow at the water/fuel oil interface. It exploits the aromatic fraction of fuel oils as a carbon and energy source. PP1Y is able to grow on a wide range of mono-, poly- and heterocyclic aromatic hydrocarbons. Here, we report the complete functional annotation of the whole Novosphingobium genome. Results PP1Y genome analysis and its comparison with other Sphingomonadal genomes has yielded novel insights into the molecular basis of PP1Y’s phenotypic traits, such as its peculiar ability to encapsulate and degrade the aromatic fraction of fuel oils. In particular, we have identified and dissected several highly …

NovosphingobiumSphingomonadDe novo sequencing; Novosphingobium sp. PP1Y; Sphingomonads; Aromatic pollutant compounds/bioremediationAromatic pollutant compoundComputational biologyNovosphingobium sp. PP1YAromatic pollutant compounds/bioremediationGenomeSphingomonadsDNA sequencingDe novo sequencingbioremediationNext generation sequencingGeneticsPhylogenyWhole genome sequencingGeneticschemistry.chemical_classificationbiologyHigh-Throughput Nucleotide SequencingQuorum SensingSequence Analysis DNAbiology.organism_classificationSphingomonadaceaeSphingomonadaceaeQuorum sensingBiodegradation EnvironmentalchemistryGenes BacterialEnergy sourceAromatic hydrocarbonMetabolic Networks and PathwaysResearch ArticleBiotechnology
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Rational Design of a Carrier Protein for the Production of Recombinant Toxic Peptides in Escherichia coli

2016

Commercial uses of bioactive peptides require low cost, effective methods for their production. We developed a new carrier protein for high yield production of recombinant peptides in Escherichia coli very well suited for the production of toxic peptides like antimicrobial peptides. GKY20, a short antimicrobial peptide derived from the C-terminus of human thrombin, was fused to the C-terminus of Onconase, a small ribonuclease (104 amino acids), which efficiently drove the peptide into inclusion bodies with very high expression levels (about 200-250 mg/L). After purification of the fusion protein by immobilized metal ion affinity chromatography, peptide was obtained by chemical cleavage in d…

Genetics and Molecular Biology (all)0301 basic medicineProtein ExpressionCarboxylic Acidslcsh:MedicinePeptideMedicine (all); Biochemistry Genetics and Molecular Biology (all); Agricultural and Biological Sciences (all)medicine.disease_causeBiochemistrylaw.inventionlawMedicine and Health SciencesAmino Acidslcsh:ScienceAcetic Acidchemistry.chemical_classificationAntimicrobial Cationic PeptideMultidisciplinaryAntimicrobialsOrganic CompoundsHydrolysisMedicine (all)Chemical ReactionsDrugsRecombinant ProteinRecombinant ProteinsAmino acidChemistryBiochemistryPhysical SciencesRecombinant DNAHumanResearch Article030106 microbiologyAntimicrobial peptidesResearch and Analysis MethodsMicrobiologyRibonuclease03 medical and health sciencesResidue (chemistry)RibonucleasesAffinity chromatographyMicrobial ControlGene Expression and Vector TechniquesEscherichia colimedicineSulfur Containing Amino AcidsHumansCysteineMolecular Biology TechniquesMolecular BiologyEscherichia coliPharmacologyMolecular Biology Assays and Analysis TechniquesBiochemistry Genetics and Molecular Biology (all)lcsh:ROrganic ChemistryFormic AcidChemical CompoundsBiology and Life SciencesProteins030104 developmental biologyAgricultural and Biological Sciences (all)chemistrylcsh:QCarrier ProteinPeptidesCarrier ProteinsAcidsAntimicrobial Cationic PeptidesCysteinePLOS ONE
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