Search results for " Streptomyces"

showing 9 items of 19 documents

Artificial chromosome libraries of Streptomyces coelicolor A3(2) and Planobispora rosea

2003

Using an Escherichia coli-Streptomyces shuttle vector derived from a bacterial artificial chromosome (BAC), we developed methodologies for the construction of BAC libraries of filamentous actinomycetes. Libraries of Streptomyces coelicolor, the model actinomycete, and Planobispora rosea, a genetically intractable strain, were constructed. Both libraries have an average insert size of 60 kb, with maximal insert larger than 150 kb. The S. coelicolor library was evaluated by selected hybridisations to DraI fragments and by end sequencing of a few clones. Hybridisation of the P. rosea library to selected probes indicates a good representation of the P. rosea genome and that the library can be u…

GeneticsQuality ControlBacterial artificial chromosomeChromosomes Artificial BacterialChromosomes Artificial Bacterial; Molecular Biology; Quality Control; Streptomyces; Gene LibrarybiologyStreptomyces coelicolorbiology.organism_classificationMicrobiologyStreptomycesGenomeInsert (molecular biology)StreptomycesShuttle vectorStreptomyceGeneticsGenomic libraryActinomycetalesMolecular BiologyGene Library
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New Tetromycin Derivatives with Anti-Trypanosomal and Protease Inhibitory Activities

2011

Four new tetromycin derivatives, tetromycins 1-4 and a previously known one, tetromycin B (5) were isolated from Streptomyces axinellae Pol001(T) cultivated from the Mediterranean sponge Axinella polypoides. Structures were assigned using extensive 1D and 2D NMR spectroscopy as well as HRESIMS analysis. The compounds were tested for antiparasitic activities against Leishmania major and Trypanosoma brucei, and for protease inhibition against several cysteine proteases such as falcipain, rhodesain, cathepsin L, cathepsin B, and viral proteases SARS-CoV M(pro), and PL(pro). The compounds showed antiparasitic activities against T. brucei and time-dependent inhibition of cathepsin L-like proteas…

Magnetic Resonance Spectroscopyanti-trypanosomalmedicine.medical_treatmentCathepsin LStreptomyces axinellaePharmaceutical ScienceCathepsin BCathepsin BCathepsin LCathepsin ODrug DiscoveryPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5Coronavirus 3C ProteasesLeishmania major0303 health sciencesbiology030302 biochemistry & molecular biologytetromycin; anti-trypanosomal; protease inhibition; <em>Streptomyces axinellae</em>; marine spongeTrypanocidal AgentsStreptomycesCysteine EndopeptidasesBiochemistrySevere acute respiratory syndrome-related coronavirusStreptomyces axinellaetetromycinBiologiemarine spongeddc:547ProteasesTrypanosoma brucei bruceiAntiprotozoal AgentsTrypanosoma bruceiHeterocyclic Compounds 4 or More RingsArticle03 medical and health sciencesViral ProteinsAxinellaparasitic diseasesmedicineAnimalsProtease Inhibitorsddc:610protease inhibition ; anti-trypanosomal ; Streptomyces axinellae ; tetromycin ; marine sponge030304 developmental biologyCathepsinProteasebiology.organism_classificationprotease inhibitionlcsh:Biology (General)biology.protein
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The Streptomyces coelicolor Small ORF trpM Stimulates Growth and Morphological Development and Exerts Opposite Effects on Actinorhodin and Calcium-De…

2020

In actinomycetes, antibiotic production is often associated with a morpho-physiological differentiation program that is regulated by complex molecular and metabolic networks. Many aspects of these regulatory circuits have been already elucidated and many others still deserve further investigations. In this regard, the possible role of many small open reading frames (smORFs) in actinomycete morpho-physiological differentiation is still elusive. In Streptomyces coelicolor, inactivation of the smORF trpM (SCO2038) – whose product modulates L-tryptophan biosynthesis – impairs production of antibiotics and morphological differentiation. Indeed, it was demonstrated that TrpM is able to interact w…

Microbiology (medical)Primary and secondary metabolismlcsh:QR1-502cytosol aminopeptidaseStreptomyces coelicoloractinorhodin productionSettore BIO/19 - Microbiologia GeneraletrpM.MicrobiologyAminopeptidaselcsh:MicrobiologyActinorhodin03 medical and health scienceschemistry.chemical_compoundBiosynthesisTRPMSmall open reading frameProtein biosynthesis030304 developmental biologychemistry.chemical_classificationsmall open reading frame0303 health sciencescalcium-dependent antibioticCalcium-dependent antibioticbiologysmall open reading frame trpM actinorhodin production Streptomyces coelicolor cytosol aminopeptidase calcium-dependent antibiotic primary and secondary metabolism030306 microbiologyActinorhodin productionStreptomyces coelicolorprimary and secondary metabolismtrpMbiology.organism_classificationAmino acidMetabolic pathwaychemistryBiochemistryCytosol aminopeptidaseFrontiers in Microbiology
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Proteomics highlights metabolic changes associated with n-hexadecane utilization in a Streptomyces coelicolor engineered strain.

2011

Proteomics n-hexadecane utilization Streptomyces coelicolor genetically engineered strain.
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TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2).

2016

In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was rescued by tryptophan and tryptophan precursor (serine and/or indole) su…

Proteomics0301 basic medicineProtein ExtractionMutantlcsh:MedicineStreptomyces coelicolor A3(2)Settore BIO/19 - Microbiologia GeneraleBiochemistrySerinechemistry.chemical_compoundAromatic Amino AcidsSmall ProteinAntibioticsTRPMMicrobial PhysiologyMedicine and Health SciencesBacterial PhysiologyAmino Acidslcsh:ScienceProtein MetabolismExtraction TechniquesMultidisciplinarybiologyOrganic CompoundsAntimicrobialsStreptomyces coelicolorTryptophanDrugsChemistryBiochemistryPhysical SciencesPhysiological DifferentiationResearch ArticleTryptophan BiosynthesiSmall Protein; Biosynthesis; Morpho-Physiological Differentiation: Streptomyces coelicolorBiosynthesisResearch and Analysis MethodsMicrobiologyStreptomycesActinorhodin03 medical and health sciencesBiosynthesisMicrobial ControlBacterial SporesPharmacology030102 biochemistry & molecular biologyOrganic Chemistrylcsh:RChemical CompoundsTryptophanTrpM; Small Protein; Tryptophan Biosynthesis; Morphological Differentiation; Physiological Differentiation; Streptomyces coelicolor A3(2); ProteomicsBiology and Life SciencesProteinsBacteriologybiology.organism_classificationAmino Acid MetabolismMetabolism030104 developmental biologychemistrylcsh:QMorphological DifferentiationTrpM
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The Histidinol Phosphate Phosphatase Involved in Histidine Biosynthetic Pathway Is Encoded by SCO5208 (hisN) in Streptomyces coelicolor A3(2)

2008

Through the screening of a Streptomyces coelicolor genomic library, carried out in a histidinol phosphate phosphatase (HolPase) deficient strain, SCO5208 was identified as the last unknown gene involved in histidine biosynthesis. SCO5208 is a phosphatase, and it can restore the growth in minimal medium in this HolPase deficient strain when cloned in a high or low copy number vector. Moreover, it shares sequence homology with other HolPases recently identified in Actinobacteria. During this work a second phosphatase, SCO2771, sharing no homologies with SCO5208 and all so far described phosphatases was identified. It can complement HolPase activity mutation only at high copy number. Sequence …

Sequence analysisPhosphataseDNA Mutational AnalysisMolecular Sequence DataMutation MissenseStreptomyces coelicolormedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyBacterial ProteinsHistidinol Phosphate Phosphatase Histidine Biosynthesis Streptomyces coelicolormedicineGenomic libraryHistidineAmino Acid SequenceGeneHistidineGeneticsMutationbiologySequence Homology Amino AcidStreptomyces coelicolorGenetic Complementation TestHistidinol-PhosphataseGeneral Medicinebiology.organism_classificationBiosynthetic PathwaysBiochemistryMutant ProteinsLow copy number
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Actinorhodin production intensification by nanofibrous membranes in Streptomyces coelicolor cultures

2016

In this work, electrospun polycaprolactone (PCL) and polylactic acid (PLA) membranes, subjected or not to O2-plasma treatment, werwe used as support for cell-immobilization in S. coelicolor immobilized-cells created a compact biofilm on both kinds of membranes.

Settore ING-IND/22 - Scienza E Tecnologia Dei Materialiimmobilization of Streptomyces coelicoloractinorhodin productionpolycaprolactone and polylactic acid membranesSettore BIO/19 - Microbiologia Generale
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Stategie metaboliche indotte dal triptofano in Streptomyces coelicolor

2013

Triptophan Streptomyces coelicolor metabolism
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Gordonia sp. SoCg alkB gene confers the ability to degrade and use n-alkanes as carbon source in Gram positive bacteria

2010

Gordonia sp. SoCg, a Gram positive strain able to grow on long chain n-alkanes1, possess a single copy of alkB2 gene, whose product is required for n-alkane hydroxylation3. An analysis of alkB flanking regions revealed five ORFs which were designed as orf1, rubA3, rubA4, rubB and alkU, according to the sequence 14 homology with that of known alk clusters3. In G. sp. SoCg the transcription of these genes was induced by long-chain and solid n-alkanes as revealed by quantitative RT-PCR, and the essential role of alkB in nalkane degradation was demonstrated by the construction of an alkB disruption mutant strain3. The SoCg alkB gene was successfully expressed in Streptomyces coelicolor M145 (M1…

long-chain n-alkanes Gordonia sp. Streptomyces sp. 2D-DIGEalk genesSettore BIO/19 - Microbiologia Generaleproteomic
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