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[PMID]:28455804
[Au] Autor:Zhang C; Sun X; Xu SH; Yu BY; Zhang J
[Ad] Endereço:State Key Laboratory of Natural Medicines, China Pharmaceutical University, Nanjing, Jiangsu, 210009, China.
[Ti] Título: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] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo: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] Termos MeSH primário: Biocatálise
Colchicina/química
Colchicina/metabolismo
Poluentes Ambientais/química
Poluentes Ambientais/metabolismo
Streptomyces griseus/metabolismo
[Mh] Termos MeSH secundário: Biotransformação
Metilação
Estereoisomerismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Environmental Pollutants); SML2Y3J35T (Colchicine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1007/s12010-017-2480-x


  2 / 1042 MEDLINE  
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[PMID]:28591487
[Au] Autor:Lee M; Hesek D; Lastochkin E; Dik DA; Boggess B; Mobashery S
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556, USA.
[Ti] Título: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] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo: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] Termos MeSH primário: Bactérias/metabolismo
Parede Celular/metabolismo
Enzimas/metabolismo
[Mh] Termos MeSH secundário: Biocatálise
Cromatografia Líquida de Alta Pressão
Endopeptidases/genética
Endopeptidases/metabolismo
Enzimas/genética
Glicosídeo Hidrolases/genética
Glicosídeo Hidrolases/metabolismo
Espectrometria de Massas
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Peptidoglicano/análise
Peptidoglicano/química
Peptidoglicano/metabolismo
Pseudomonas aeruginosa/enzimologia
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Streptomyces griseus/enzimologia
Especificidade por Substrato
Transferases/genética
Transferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
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] Mês de entrada:1709
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE
[do] DOI:10.1002/cbic.201700293


  3 / 1042 MEDLINE  
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[PMID]:28476986
[Au] Autor:Baygar T; Ugur A
[Ad] Endereço:Research Laboratories Center, Mugla Sitki Kocman University, 48000 Mugla, Turkey.
[Ti] Título: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] País de publicação:England
[La] Idioma:eng
[Ab] Resumo: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] Termos MeSH primário: Antioxidantes/química
Depuradores de Radicais Livres/química
Nanopartículas Metálicas/química
Prata/química
Microbiologia do Solo
Streptomyces griseus/metabolismo
[Mh] Termos MeSH secundário: Produtos Biológicos/administração & dosagem
Produtos Biológicos/química
Relação Dose-Resposta a Droga
Teste de Materiais
Nanopartículas Metálicas/ultraestrutura
Tamanho da Partícula
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Biological Products); 0 (Free Radical Scavengers); 3M4G523W1G (Silver)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170507
[St] Status:MEDLINE
[do] DOI:10.1049/iet-nbt.2015.0127


  4 / 1042 MEDLINE  
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[PMID]:28378221
[Au] Autor:Saini P; Kumar N; Wani SI; Sharma S; Chimni SS; Sareen D
[Ad] Endereço:Department of Biochemistry, Panjab University, Sector 25, Chandigarh, 160 014, India.
[Ti] Título:Bioresolution of racemic phenyl glycidyl ether by a putative recombinant epoxide hydrolase from Streptomyces griseus NBRC 13350.
[So] Source:World J Microbiol Biotechnol;33(5):82, 2017 May.
[Is] ISSN:1573-0972
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:In order to produce enantiomerically pure epoxides for the synthesis of value-added chemicals, a novel putative epoxide hydrolase (EH) sgeh was cloned and overexpressed in pET28a/Escherichia coli BL21(DE3). The 1047 bp sgeh gene was mined from Streptomyces griseus NBRC 13350 genome sequence. The recombinant hexahistidyl-tagged SGEH was purified (16.6-fold) by immobilized metal-affinity chromatography, with 90% yield as a homodimer of 100 kDa. The recombinant E. coli whole cells overexpressing SGEH could kinetically resolve racemic phenyl glycidyl ether (PGE) into (R)-PGE with 98% ee, 40% yield, and enantiomeric ratio (E) of 20. This was achieved under the optimized reaction conditions i.e. cell/substrate ratio of 20:1 (w/w) at pH 7.5 and 20 °C in 10% (v/v) dimethylformamide (DMF) in a 10 h reaction. 99% enantiopure (R)-PGE was obtained when the reaction time was prolonged to 12 h with a yield of 34%. In conclusion, an economically viable and environment friendly green process for the production of enantiopure (R)-PGE was developed by using wet cells of E. coli expressing recombinant SGEH.
[Mh] Termos MeSH primário: Epóxido Hidrolases/metabolismo
Éteres Fenílicos/metabolismo
Streptomyces griseus/enzimologia
[Mh] Termos MeSH secundário: Cromatografia em Gel
Clonagem Molecular
Epóxido Hidrolases/genética
Escherichia coli/genética
Cinética
Proteínas Recombinantes/metabolismo
Estereoisomerismo
Streptomyces griseus/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phenyl Ethers); 0 (Recombinant Proteins); 44KJQ1655I (phenylglycidyl ether); EC 3.3.2.- (Epoxide Hydrolases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1007/s11274-017-2248-z


  5 / 1042 MEDLINE  
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[PMID]:28161545
[Au] Autor:Kumar P; Ryan B; Henehan GT
[Ad] Endereço:School of Food Science and Environmental Health, College of Science and Health, Dublin Institute of Technology, Dublin 1, Ireland.
[Ti] Título:ß-Glucosidase from Streptomyces griseus: Nanoparticle immobilisation and application to alkyl glucoside synthesis.
[So] Source:Protein Expr Purif;132:164-170, 2017 Apr.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A novel ß-glucosidase from Streptomyces griseus was cloned and overexpressed in E. coli. The purified ß-glucosidase (44 kDa) had a K of 8.6 ± 0.5 mM and a V of 217 ± 5.0 µmoles min mg at 37 °C, pH 7.2 with p-nitrophenyl-ß-D glucopyranoside as substrate. The enzyme was characterised in terms of pH optimum (pH 6.9), temperature optimum (69 °C) and the influence of solvents and effectors. Purified S. griseus ß-glucosidase was successfully immobilised, by simple absorption, onto zinc oxide (ZnO) nanoparticles without covalent modification. It remained tightly bound even after extensive washing and could be reused up to ten times without significant loss of activity. The immobilised enzyme had a higher optimum temperature and greater thermostability than the free enzyme. In immobilised form the enzyme readily catalysed the synthesis of alkyl glucosides.
[Mh] Termos MeSH primário: Proteínas de Bactérias
Glucosídeos/síntese química
Nanopartículas/química
Streptomyces griseus/genética
beta-Glucosidase
[Mh] Termos MeSH secundário: Proteínas de Bactérias/biossíntese
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/isolamento & purificação
Glucosídeos/química
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Streptomyces griseus/enzimologia
beta-Glucosidase/biossíntese
beta-Glucosidase/química
beta-Glucosidase/genética
beta-Glucosidase/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Glucosides); 0 (Recombinant Proteins); EC 3.2.1.21 (beta-Glucosidase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170703
[Lr] Data última revisão:
170703
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170206
[St] Status:MEDLINE


  6 / 1042 MEDLINE  
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[PMID]:27691921
[Au] Autor:Takano H; Matsui Y; Nomura J; Fujimoto M; Katsumata N; Koyama T; Mizuno I; Amano S; Shiratori-Takano H; Komatsu M; Ikeda H; Ueda K
[Ad] Endereço:a Life Science Research Center, College of Bioresource Sciences, Nihon University , Fujisawa , Japan.
[Ti] Título:High production of a class III lantipeptide AmfS in Streptomyces griseus.
[So] Source:Biosci Biotechnol Biochem;81(1):153-164, 2017 Jan.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AmfS, a class III lantipeptide serves as a morphogen in Streptomyces griseus. Here, we constructed a high production system of AmfS in S. griseus. We isolated S. griseus Grd1 strain defective in glucose repression of aerial mycelium formation and found it suitable for the overproduction of AmfS. Two expression vectors carrying the strong and constitutive ermE2 promoter were constructed using a multicopy number plasmid, pIJ702. The use of the Grd1 strain combined with the expression vectors enabled high production of AmfS by S. griseus into its culture broth. The expression system was also effective for the generation of abundant AmfS derived from Streptomyces avermitilis. In addition, site-directed mutagenesis revealed the amino acid residues essential for the morphogen activity of AmfS. These results indicate that the constructed system enables efficient production of class III lantipeptides by Streptomyces.
[Mh] Termos MeSH primário: Proteínas de Bactérias/biossíntese
Engenharia Genética
Streptomyces griseus/genética
Streptomyces griseus/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Vetores Genéticos/genética
Família Multigênica/genética
Mutação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AmfS protein, Streptomyces griseus); 0 (Bacterial Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170131
[Lr] Data última revisão:
170131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE


  7 / 1042 MEDLINE  
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[PMID]:27702481
[Au] Autor:Tan Z; Ma H; Li Q; Pu L; Cao Y; Qu X; Zhu C; Ying H
[Ad] Endereço:College of Biotechnology and Pharmaceutical Engineering, Nanjing Tech University, Nanjing, China; National Engineering Technique Research Center for Biotechnology, Nanjing, China.
[Ti] Título:Biosynthesis of optically pure chiral alcohols by a substrate coupled and biphasic system with a short-chain dehydrogenase from Streptomyces griseus.
[So] Source:Enzyme Microb Technol;93-94:191-199, 2016 Nov.
[Is] ISSN:1879-0909
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The increasing demand for biocatalysts in synthesizing enantiomerically pure chiral alcohols results from the outstanding characteristics of enzymes in reaction, economic, ecological issues. Many carbonyl reductases for producing chiral alcohols have been reported but there is still a lack of good catalytic efficacies. Herein, five carbonyl reductases from different Streptomyces were discovered by the strategy of genome mining. These reductases were overexpressed, and we chose SgCR for further study as it owned better enzyme activity. This protein was purified to apparent homogeneity, and its amino acid sequence was analyzed in comparison with that of the reported SDRs. The biocatalytic properties of SgCR were investigated, and this enzyme was confirmed to have the ability to convert various prochiral ketones into highly optically active alcohols. SgCR exhibited the highest activity towards ethyl 4-chloro-3-oxobutanoate (COBE) and the corresponding product ethyl (S)-4-chloro-3-hydroxybutanoate ((S)-CHBE) was obtained with high yield and excellent e.e. value by optimizing the biphasic system. Eventually, using isopropanol as the co-substrate for NADH recycling in the substrate-coupled reaction, the yield and enantioselectivity of (S)-CHBE were obtained at the values of 90% and 99%, respectively. These results indicate that SgCR is a promising boicatalyst for the synthesis of chiral alcohols in industry.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/metabolismo
Álcoois/metabolismo
Proteínas de Bactérias/metabolismo
Streptomyces griseus/enzimologia
[Mh] Termos MeSH secundário: Oxirredutases do Álcool/química
Oxirredutases do Álcool/genética
Álcoois/química
Sequência de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Biocatálise
Mineração de Dados
Estabilidade Enzimática
Genoma Bacteriano
Cinética
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
Estereoisomerismo
Streptomyces griseus/genética
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alcohols); 0 (Bacterial Proteins); 0 (Recombinant Proteins); EC 1.1.- (Alcohol Oxidoreductases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE


  8 / 1042 MEDLINE  
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[PMID]:27444385
[Au] Autor:Li M; Chen Y; Wu S; Tang Y; Deng Y; Yuan J; Dong J; Li H; Tang L
[Ad] Endereço:Department of Microecology, College of Basic Medical Science, Dalian Medical University, Dalian, Liaoning 116044, China.
[Ti] Título:TmcN is involved in ATP regulation of tautomycetin biosynthesis in Streptomyces griseochromogenes.
[So] Source:Biochem Biophys Res Commun;478(1):221-226, 2016 09 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The regulatory mechanism of tautomycetin (TMC) biosynthesis remains largely unknown, although it has been of great interest to the pharmaceutical industry. Our previous study showed that intracellular adenosine triphosphate (inATP) level is negatively correlated with secondary metabolite biosynthesis in various Streptomyces spp. In this study, by exogenous treatment of ATP, we also found a negative correlation between TMC biosynthesis and inATP level in Streptomyces griseochromogenes (S. griseochromogenes). However, the underlying mechanism remains unclear. TmcN, a pathway-specific transcriptional regulator of TMC biosynthetic genes, was previously revealed as a large ATP-binding LuxR (LAL) family protein. The predicted amino acid sequence of TmcN shows highly conserved Walker A and B binding motifs, which suggest an ATPase function of TmcN. We therefore hypothesized that the ATPase domain of TmcN may play a role in sensing endogenous pool of ATP, and is thus involved in the ATP regulation of TMC biosynthesis. To test the hypothesis, we first explored the key residue that affects the ATPase activity of TmcN by amino acid sequence alignment and structural simulation. After that, we disrupted tmcN gene in S. griseochromogenes, and the tmcN or site-direct-mutated tmcN were re-introduced to get the complementary and ATPase domain disrupted strains. The transcription level of tmcN, TMC yield, and inATP, as well as the effect of ATP on TMC production of different mutants were evaluated. Deletion of tmcN or site-direct mutation of ATPase domain of TmcN in S. griseochromogenes significantly reduced the TMC production, and it was not affected by exogenous ATP treatment. In addition, a relatively high level of inATP was detected in tmcN deletion and site-direct mutation strains. Our results here suggested that TmcN, especially its ATPase domain, is involved in consuming of endogenous ATP pool and thus plays pivotal role in connecting the primary and secondary metabolite in S. griseochromogenes.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/metabolismo
Regulação Bacteriana da Expressão Gênica/fisiologia
Lipídeos/biossíntese
Streptomyces griseus/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Furanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Furans); 0 (Lipids); 0 (Transcription Factors); 119757-73-2 (tautomycetin); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171126
[Lr] Data última revisão:
171126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160723
[St] Status:MEDLINE


  9 / 1042 MEDLINE  
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[PMID]:27405846
[Au] Autor:Zhan Y; Zheng S
[Ad] Endereço:School of Life and Environmental Sciences, Guilin University of Electronic Technology, Guilin 541004, People's Republic of China.
[Ti] Título:Efficient production of nonactin by Streptomyces griseus subsp. griseus.
[So] Source:Can J Microbiol;62(8):711-4, 2016 Aug.
[Is] ISSN:1480-3275
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Here we report the production of the cyclic macrotetrolide nonactin from the fermentation culture of Streptomyces griseus subsp. griseus. Nonactin is a member of a family of naturally occurring cyclic ionophores known as the macrotetrolide antibiotics. Our fermentation procedure of Streptomyces griseus was performed at 30 °C and 200 rev·min(-1) for 5 days on a rotary shaker. Diaion HP-20 and Amberlite XAD-16 were added to the fermentation medium. Isolated yield of nonactin was up to 80 mg·L(-1) using our methodology. Nonactin is commonly known as an ammonium ionophore and also exhibits antibacterial, antiviral, and antitumor activities. It is also widely used for the preparation of ion-selective electrodes and sensors. Chemical synthesis of nonactin has been achieved by some groups; however, overall yields are very low, making efficient biosynthesis an attractive means of production.
[Mh] Termos MeSH primário: Antibacterianos/metabolismo
Streptomyces griseus/metabolismo
[Mh] Termos MeSH secundário: Antibacterianos/química
Fermentação
Macrolídeos/química
Macrolídeos/metabolismo
Polímeros
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Macrolides); 0 (Polymers); 104219-63-8 (Amberlite XAD-16); TTP24WX8P7 (nonactin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170113
[Lr] Data última revisão:
170113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160714
[St] Status:MEDLINE
[do] DOI:10.1139/cjm-2016-0248


  10 / 1042 MEDLINE  
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[PMID]:27268270
[Au] Autor:Takano H; Toriumi N; Hirata M; Amano T; Ohya T; Shimada R; Kusada H; Amano S; Matsuda K; Beppu T; Ueda K
[Ad] Endereço:Life Science Research Center, College of Bioresource Sciences, Nihon University, 1866 Kameino, Fujisawa 252-0880, Japan takano.hideaki@nihon-u.ac.jp.
[Ti] Título:An ABC transporter involved in the control of streptomycin production in Streptomyces griseus.
[So] Source:FEMS Microbiol Lett;363(14), 2016 Jul.
[Is] ISSN:1574-6968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We screened for a gene that inhibits streptomycin production in Streptomyces griseus when it is introduced on a high-copy-number plasmid pIJ702, and obtained a plasmid pKM545. The introduction of pKM545 abolished streptomycin production on all media tested including YMP-sugar and Nutrient broth. S1 protection analysis demonstrated that the introduction of this plasmid downregulated the transcriptional activity of the promoter preceding strR, the pathway-specific transcriptional regulator for streptomycin biosynthesis. The 2.8-kb BamHI fragment cloned onto pKM545 contained two coding sequences SGR_5442 and 5443. These coding sequences and the two downstream ones (SGR_5444 and 5445) constituted a possible operon structure designated to be rspABCD (regulation of streptomycin production). RspB and RspC exhibited a marked similarity with an ATP-binding domain and a membrane-associating domain of an ABC-2 type transporter, respectively, suggesting that the Rsp proteins comprise a membrane exporter. The gene cluster consisting of the rsp operon and the upstream divergent small coding sequence (SGR_5441) was widely distributed to Streptomyces genome. An rspB mutant of S. griseus produced 3-fold streptomycin of the parental strain in YMP liquid medium. The evidence implies that the Rsp translocator is involved in the export of a substance that specifies the expression level of streptomycin biosynthesis genes in S. griseus.
[Mh] Termos MeSH primário: Transportadores de Cassetes de Ligação de ATP/genética
Transportadores de Cassetes de Ligação de ATP/metabolismo
Streptomyces griseus/genética
Streptomyces griseus/metabolismo
Estreptomicina/biossíntese
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Clonagem Molecular
Ordem dos Genes
Loci Gênicos
Mutação
Plasmídeos/genética
Domínios e Motivos de Interação entre Proteínas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); Y45QSO73OB (Streptomycin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160609
[St] Status:MEDLINE



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