Database : MEDLINE
Search on : streptomyces and griseus [Words]
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[PMID]: 28455804
[Au] Autor:Zhang C; Sun X; Xu SH; Yu BY; Zhang J
[Ad] Address:State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing, Jiangsu, 210009, China.
[Ti] Title:Microbial Catalyzed Regio-Selective Demethylation of Colchicine by Streptomyces griseus ATCC 13273.
[So] Source:Appl Biochem Biotechnol;183(3):1026-1034, 2017 Nov.
[Is] ISSN:1559-0291
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Colchicinoids and their derivatives are of great importance in pharmaceutical applications, and colchicine is usually used as the first choice for the treatment of gout. To expand the structural diversities and clinical application of colchicinoids, many attempts have been established for the derivatives with better activity or less toxicity. Herein, in this paper, we report a direct microbial transformation of colchicine into 2-O-demethyl-colchicine (M1) and 3-O-demethl-colchicine (M2) by Streptomyces griseus ATCC 13273. It is noteworthy that when DMF was used as co-solvent, the yield of M1 and M2 could reach up to 51 and 31%, respectively. All the structures of the metabolites were elucidated unambiguously by ESI-MS, H-NMR, C-NMR, and 2D-NMR spectroscopy.
[Mh] MeSH terms primary: Biocatalysis
Colchicine/chemistry
Colchicine/metabolism
Environmental Pollutants/chemistry
Environmental Pollutants/metabolism
Streptomyces griseus/metabolism
[Mh] MeSH terms secundary: Biotransformation
Methylation
Stereoisomerism
Substrate Specificity
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Environmental Pollutants); SML2Y3J35T (Colchicine)
[Em] Entry month:1711
[Cu] Class update date: 171128
[Lr] Last revision date:171128
[Js] Journal subset:IM
[Da] Date of entry for processing:170430
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-017-2480-x

  2 / 1563 MEDLINE  
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[PMID]: 29061030
[Au] Autor:Chi WJ
[Ad] Address:Biological and Genetic Resources Assessment Division, National Institute of Biological Resources, Incheon 22689, Korea.
[Ti] Title:DasR, a GntR-family global regulator, regulates -acetylglucosamine metabolism in Streptomyces griseus.
[So] Source:J Microbiol Biotechnol;, 2017 Oct 25.
[Is] ISSN:1738-8872
[Cp] Country of publication:Korea (South)
[La] Language:eng
[Ab] Abstract:DasR is divergently encoded upstream of , which itself encodes a substrate-binding protein of an ATP-binding cassette (ABC) transport system. As determined by DNase I footprinting using recombinant DasR prepared from Escherichia coli, DasR bound to two operator sequences- located at nucleotide positions -22 to -13, with respect to the transcriptional start point of , and located at positions +3 to +12. Gel-mobility shift assays using the DNA fragments containing one or both of the two operator sequences suggested that a DasR dimer bound first to and the DNA-bound DasR recruited another dimer to , resulting in the formation of a stable DNA-protein complex that prevented RNA polymerase from binding to the promoter. DasR was bound upstream of genes encoding an -acetylglucosamine transport system and a chitinolytic system. Transcription of these genes was derepressed in the -disrupted mutant. These results suggest that DasR is a global regulator in metabolism of monomeric and polymeric forms of -acetylglucosamine in .
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1710
[Cu] Class update date: 171024
[Lr] Last revision date:171024
[St] Status:Publisher
[do] DOI:10.4014/jmb.1708.08026

  3 / 1563 MEDLINE  
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[PMID]: 28980921
[Au] Autor:Yu CH; Wang H; Wang Y; Cui NX; Zhao X; Rong L; Yi ZC
[Ad] Address:School of Biological Science and Medical Engineering, Beihang University, 37 Xueyuan Road, Beijing 100191, China.
[Ti] Title:Protease sensitivity and redistribution of CD71 and glycophorin A on K562 cells.
[So] Source:Cell Mol Biol (Noisy-le-grand);63(9):40-45, 2017 Sep 30.
[Is] ISSN:1165-158X
[Cp] Country of publication:France
[La] Language:eng
[Ab] Abstract:Transmembrane proteins are delivered to plasma membrane from the endoplasmic reticulum and Golgi complex by vesicular transport along with the cytoskeletal network. Disruption of this process likely affects transmembrane protein expression. K562 cells were digested with Streptomyces griseus protease for different periods of time, and then re-cultured with different cytoskeletal and glycosylation inhibitors. Cell viability and surface expression of transferrin receptor (CD71) and glycophorin A (GPA) were analyzed before and after re-culture by flow cytometry. We found that digestion with protease almost completely removed extracellular CD71 and GPA but their expression recovered to the initial levels after re-culture for 8 h and 24 h, respectively. The microtubule depolymerizer colchicine promoted cell surface recovery of CD71 but inhibited that of GPA; the microtubule stabilizer paclitaxel inhibited cell surface recovery of CD71 but promoted that of GPA; the microfilament depolymerizer cytochalasin D had no effect on cell surface recovery of CD71 and GPA; the microfilament stabilizer phalloidin inhibited cell surface recovery of GPA. The glycosylation inhibitor tunicamycin inhibited the recovery of both CD71 and GPA, and BADGP inhibited the recovery of GPA. These studies show differential sensitivities of surface proteins on K562 cells to proteases, and suggest molecular mechanisms of transmembrane protein transport and cycling.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1710
[Cu] Class update date: 171005
[Lr] Last revision date:171005
[St] Status:In-Process
[do] DOI:10.14715/cmb/2017.63.9.8

  4 / 1563 MEDLINE  
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[PMID]: 28946098
[Au] Autor:Zhang Y; Huang H; Yao X; Du G; Chen J; Kang Z
[Ad] Address:Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu 214122, China; Synergetic Innovation Center of Food Safety and Nutrition, 1800 Lihu Road, Wuxi, Jiangsu 214122, China.
[Ti] Title:High-yield secretory production of stable, active trypsin through engineering of the N-terminal peptide and self-degradation sites in Pichia pastoris.
[So] Source:Bioresour Technol;247:81-87, 2017 Aug 04.
[Is] ISSN:1873-2976
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Streptomyces griseus trypsin (SGT) possesses enzymatic properties similar to mammalian trypsins and has great potential applications in the leather processing, bioethanol, detergent and pharmaceutical industry. Here, a new strategy was reported for improving its stable, active secretory production through engineering of its propeptide and self-degradation sites. By rationally introducing hydrophobic mutations into the N-terminus of SGT Exmt (R145I), replacing the propeptide with FPVDDDDK and engineering the α-factor signal peptide, trypsin production (amidase activity) was improved to 177.85±2.83U·mL in a 3-L fermenter (a 3.75-fold increase). Subsequently, all of the residues involved in autolysis that were identified by mass spectrometry were mutated and the resulting proteins were evaluated. In particular, the variant tbcf (K101A) demonstrated high stability and production (227.65±6.51U·mL and 185.71±5.68mg·L , respectively). The recombinant strain constructed here has great potential for large-scale production of active trypsin.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1709
[Cu] Class update date: 170925
[Lr] Last revision date:170925
[St] Status:Publisher

  5 / 1563 MEDLINE  
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[PMID]: 28942636
[Au] Autor:Yu N; Lobue PA; Cao X; Limbach PA
[Ad] Address:Rieveschl Laboratories for Mass Spectrometry, Department of Chemistry, University of Cincinnati , P.O. Box 210172, Cincinnati, Ohio 45221-0172, United States.
[Ti] Title:RNAModMapper: RNA Modification Mapping Software for Analysis of Liquid Chromatography Tandem Mass Spectrometry Data.
[So] Source:Anal Chem;89(20):10744-10752, 2017 Oct 17.
[Is] ISSN:1520-6882
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Liquid chromatography tandem mass spectrometry (LC-MS/MS) has proven to be a powerful analytical tool for the characterization of modified ribonucleic acids (RNAs). The typical approach for analyzing modified nucleosides within RNA sequences by mass spectrometry involves ribonuclease digestion followed by LC-MS/MS analysis and data interpretation. Here we describe a new software tool, RNAModMapper (RAMM), to assist in the interpretation of LC-MS/MS data. RAMM is a stand-alone package that requires user-submitted DNA or RNA sequences to create a local database against which collision-induced dissociation (CID) data of modified oligonucleotides can be compared. RAMM can interpret MS/MS data containing modified nucleosides in two modes: fixed and variable. In addition, RAMM can also utilize interpreted MS/MS data for RNA modification mapping back against the input sequence(s). The applicability of RAMM was first tested using total tRNA isolated from Escherichia coli. It was then applied to map modifications found in 16S and 23S rRNA from Streptomyces griseus.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1709
[Cu] Class update date: 171017
[Lr] Last revision date:171017
[St] Status:In-Data-Review
[do] DOI:10.1021/acs.analchem.7b01780

  6 / 1563 MEDLINE  
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[PMID]: 28634080
[Au] Autor:Park W; Woo JK; Shin J; Oh KB
[Ad] Address:Department of Agricultural Biotechnology, College of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Republic of Korea.
[Ti] Title:nonG, a constituent of the nonactin biosynthetic gene cluster, regulates nocardamine synthesis in Streptomyces albus J1074.
[So] Source:Biochem Biophys Res Commun;490(3):664-669, 2017 Aug 26.
[Is] ISSN:1090-2104
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Many factors regulate the expression of specialised secondary metabolite biosynthetic gene clusters, which have been recognised as important for the discovery of novel microbial natural products. A cosmid library based on genomic DNA of the marine-derived Streptomyces puniceus Act1085 was constructed and screened to identify a short gene cluster similar to the nonactin biosynthetic cluster. The ORFs of the gene cluster isolated had high amino acid sequence identity, from 82% to 96%, with corresponding ORFs of the nonactin biosynthetic gene cluster from S. griseus subsp. griseus ETH A7796. Despite the expectation that nonactin or its derivatives would be made from heterologous expression of the gene cluster found in S. albus J1074, nocardamine was isolated. The heterologous expression data indicate that the production of nocardamine in S. albus J1074 is due to an ortholog of nonG, a TetR family transcriptional regulator, from S. puniceus Act1085.
[Mh] MeSH terms primary: Biosynthetic Pathways
Genes, Bacterial
Multigene Family
Peptides, Cyclic/metabolism
Streptomyces/genetics
[Mh] MeSH terms secundary: Cloning, Molecular
Gene Expression
Macrolides/metabolism
Peptides, Cyclic/genetics
Streptomyces/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Macrolides); 0 (Peptides, Cyclic); Q645668975 (deferrioxamine E); TTP24WX8P7 (nonactin)
[Em] Entry month:1708
[Cu] Class update date: 170811
[Lr] Last revision date:170811
[Js] Journal subset:IM
[Da] Date of entry for processing:170622
[St] Status:MEDLINE

  7 / 1563 MEDLINE  
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[PMID]: 28595598
[Au] Autor:Hoza AS; Mfinanga SGS; Moser I; König B
[Ad] Address:Department of Medical Microbiology and Epidemiology of Infectious Diseases, Faculty of Medicine, University of Leipzig, Liebig Str. 21, 04103, Leipzig, Germany. abshoza@gmail.com.
[Ti] Title:Isolation, biochemical and molecular identification of Nocardia species among TB suspects in northeastern, Tanzania; a forgotten or neglected threat?
[So] Source:BMC Infect Dis;17(1):407, 2017 Jun 08.
[Is] ISSN:1471-2334
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:BACKGROUND: Pulmonary nocardiosis mimic pulmonary tuberculosis in most clinical and radiological manifestations. In Tanzania, where tuberculosis is one of the major public health threat clinical impact of nocardiosis as the cause of the human disease remains unknown. The objective of the present study was to isolate and identify Nocardia isolates recovered from TB suspects in Northeastern, Tanzania by using biochemical and molecular methods. METHODS: The study involved 744 sputum samples collected from 372 TB suspects from four periphery diagnostic centers in Northeastern, Tanzania. Twenty patients were diagnosed as having presumptively Nocardia infections based on microscopic, cultural characteristics and biomèrieux ID 32C Yeast Identification system and confirmed using 16S rRNA and hsp65 gene specific primers for Nocardia species and sequencing. RESULTS: Biochemically, the majority of the isolates were N. asteroides (n = 8/20, 40%), N. brasiliensis (n = 4/20, 20%), N. farcinica (n = 3/20, 15%), N. nova (n = 1/20, 5%). Other aerobic actinomycetales included Streptomyces cyanescens (n = 2/20, 10%), Streptomyces griseus, Actinomadura madurae each (n = 1/20, 5%). Results of 16S rRNA and hsp65 sequencing were concordant in 15/17 (88. 2%) isolates and discordant in 2/17 (11.8%) isolates. Majority of the isolates belonged to N. cyriacigeorgica and N. farcinica, four (23.5%) each. CONCLUSIONS: Our findings suggest that Nocardia species may be an important cause of pulmonary nocardiosis that is underdiagnosed or ignored. This underscores needs to consider pulmonary nocardiosis as a differential diagnosis when there is a failure of anti-TB therapy and as a possible cause of human infections.
[Mh] MeSH terms primary: Lung Diseases/microbiology
Nocardia Infections/microbiology
Nocardia/isolation & purification
Tuberculosis, Pulmonary/microbiology
[Mh] MeSH terms secundary: Actinomycetales/genetics
Actinomycetales/isolation & purification
Actinomycetales/physiology
Adult
Bacterial Proteins/genetics
DNA, Ribosomal/chemistry
DNA, Ribosomal/genetics
Diagnosis, Differential
Female
Humans
Lung Diseases/diagnosis
Lung Diseases/epidemiology
Male
Nocardia/genetics
Nocardia/metabolism
Nocardia Infections/diagnosis
Nocardia Infections/epidemiology
RNA, Ribosomal, 16S/genetics
Sequence Analysis, DNA
Sputum/microbiology
Tanzania/epidemiology
Tuberculosis, Pulmonary/diagnosis
Tuberculosis, Pulmonary/epidemiology
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Bacterial Proteins); 0 (DNA, Ribosomal); 0 (RNA, Ribosomal, 16S)
[Em] Entry month:1709
[Cu] Class update date: 170926
[Lr] Last revision date:170926
[Js] Journal subset:IM
[Da] Date of entry for processing:170610
[St] Status:MEDLINE
[do] DOI:10.1186/s12879-017-2520-8

  8 / 1563 MEDLINE  
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[PMID]: 28591487
[Au] Autor:Lee M; Hesek D; Lastochkin E; Dik DA; Boggess B; Mobashery S
[Ad] Address:Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.
[Ti] Title:Deciphering the Nature of Enzymatic Modifications of Bacterial Cell Walls.
[So] Source:Chembiochem;18(17):1696-1702, 2017 Sep 05.
[Is] ISSN:1439-7633
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:The major constituent of bacterial cell walls is peptidoglycan, which, in its crosslinked form, is a polymer of considerable complexity that encases the entire bacterium. A functional cell wall is indispensable for survival of the organism. There are several dozen enzymes that assemble and disassemble the peptidoglycan dynamically within each bacterial generation. Understanding of the nature of these transformations is critical knowledge for these events. Octasaccharide peptidoglycans were prepared and studied with seven recombinant cell-wall-active enzymes (SltB1, MltB, RlpA, mutanolysin, AmpDh2, AmpDh3, and PBP5). With the use of highly sensitive mass spectrometry methods, we described the breadth of reactions that these enzymes catalyzed with peptidoglycan and shed light on the nature of the cell wall alteration performed by these enzymes. The enzymes exhibit broadly distinct preferences for their substrate peptidoglycans in the reactions that they catalyze.
[Mh] MeSH terms primary: Bacteria/metabolism
Cell Wall/metabolism
Enzymes/metabolism
[Mh] MeSH terms secundary: Biocatalysis
Chromatography, High Pressure Liquid
Endopeptidases/genetics
Endopeptidases/metabolism
Enzymes/genetics
Glycoside Hydrolases/genetics
Glycoside Hydrolases/metabolism
Mass Spectrometry
Multienzyme Complexes/genetics
Multienzyme Complexes/metabolism
Peptidoglycan/analysis
Peptidoglycan/chemistry
Peptidoglycan/metabolism
Pseudomonas aeruginosa/enzymology
Recombinant Proteins/genetics
Recombinant Proteins/isolation & purification
Recombinant Proteins/metabolism
Streptomyces griseus/enzymology
Substrate Specificity
Transferases/genetics
Transferases/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Enzymes); 0 (Multienzyme Complexes); 0 (Peptidoglycan); 0 (Recombinant Proteins); 0 (transglycosidase enzyme system); EC 2.- (Transferases); EC 3.2.1.- (Glycoside Hydrolases); EC 3.4.- (Endopeptidases); EC 3.4.99.- (mutanolysin)
[Em] Entry month:1709
[Cu] Class update date: 171114
[Lr] Last revision date:171114
[Js] Journal subset:IM
[Da] Date of entry for processing:170608
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700293

  9 / 1563 MEDLINE  
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[PMID]: 28523731
[Au] Autor:Cho HJ; Kwon YS; Kim DR; Cho G; Hong SW; Bae DW; Kwak YS
[Ad] Address:Division of Applied Life Science (BK21 Plue) and IALS, Gyeongsang National University, Jinju, Korea.
[Ti] Title:wblE2 transcription factor in Streptomyces griseus S4-7 plays an important role in plant protection.
[So] Source:Microbiologyopen;6(5), 2017 Oct.
[Is] ISSN:2045-8827
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Streptomyces griseus S4-7 was originally isolated from the strawberry rhizosphere as a microbial agent responsible for Fusarium wilt suppressive soils. S. griseus S4-7 shows specific and pronounced antifungal activity against Fusarium oxysporum f. sp. fragariae. In the Streptomyces genus, the whi transcription factors are regulators of sporulation, cell differentiation, septation, and secondary metabolites production. wblE2 function as a regulator has emerged as a new group in whi transcription factors. In this study, we reveal the involvement of the wblE2 transcription factor in the plant-protection by S. griseus S4-7. We generated ΔwblE, ΔwblE2, ΔwhiH, and ΔwhmD gene knock-out mutants, which showed less antifungal activity both in vitro and in planta. Among the mutants, wblE2 mutant failed to protect the strawberry against the Fusarium wilt pathogen. Transcriptome analyses revealed major differences in the regulation of phenylalanine metabolism, polyketide and siderophore biosynthesis between the S4-7 and the wblE2 mutant. The results contribute to our understanding of the role of streptomycetes wblE2 genes in a natural disease suppressing system.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1705
[Cu] Class update date: 171019
[Lr] Last revision date:171019
[St] Status:In-Process
[do] DOI:10.1002/mbo3.494

  10 / 1563 MEDLINE  
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[PMID]: 28476986
[Au] Autor:Baygar T; Ugur A
[Ad] Address:Research Laboratories Center, Mugla Sitki Kocman University, 48000 Mugla, Turkey.
[Ti] Title:Biosynthesis of Silver Nanoparticles by isolated from Soil and Their Antioxidant Activity.
[So] Source:IET Nanobiotechnol;11(3):286-291, 2017 Apr.
[Is] ISSN:1751-8741
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Microbial mediated biological synthesis of metallic nanoparticles was carried out ecofriendly in the present study. Silver nanoparticles (AgNPs) were extracellularly biosynthesised from AU2 and extensively characterised by ultraviolet-visible (UV-vis) and Fourier transform infrared spectroscopy, high-resolution transmission electron microscopy, scanning electron microscopy and X-ray diffraction analysis. Elemental analysis of nanoparticles was also carried out using energy dispersive X-ray spectroscopy. The biosynthesised AgNPs showed the characteristic absorption spectra in UV-vis at 422 nm which confirmed the presence of metallic AgNPs. According to the further characterisation analysis, the biosynthesised AgNPs were found to be spherical and crystalline particles with 5-20 nm average size. Antioxidant properties of the biosynthesised AgNPs were determined by 2,2-diphenyl-1-picrylhydrazyl free radical scavenging assay and was found to increase in a dose-dependent matter. The identification of the strain was determined by molecular characterisation method using 16s rDNA sequencing. The present study is the first report on the microbial biosynthesis of AgNPs using isolated from soil and provides that the active biological components found in the cell-free culture supernatant of AU2 enable the synthesis of AgNPs.
[Mh] MeSH terms primary: Antioxidants/chemistry
Free Radical Scavengers/chemistry
Metal Nanoparticles/chemistry
Silver/chemistry
Soil Microbiology
Streptomyces griseus/metabolism
[Mh] MeSH terms secundary: Biological Products/administration & dosage
Biological Products/chemistry
Dose-Response Relationship, Drug
Materials Testing
Metal Nanoparticles/ultrastructure
Particle Size
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Antioxidants); 0 (Biological Products); 0 (Free Radical Scavengers); 3M4G523W1G (Silver)
[Em] Entry month:1708
[Cu] Class update date: 170817
[Lr] Last revision date:170817
[Js] Journal subset:IM
[Da] Date of entry for processing:170507
[St] Status:MEDLINE
[do] DOI:10.1049/iet-nbt.2015.0127


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