- Streptomyces sp. strain SK68, isolated from peanut rhizosphere, promotes growth and alleviates salt stress in tomato (Solanum lycopersicum cv. Micro-Tom)
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Karthiyaini Damodharan , Sasikumar Arunachalam Palaniyandi , Bao Le , Joo-Won Suh , Seung Hwan Yang
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J. Microbiol. 2018;56(10):753-759. Published online September 28, 2018
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DOI: https://doi.org/10.1007/s12275-018-8120-5
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A novel actinobacterium, strain SK68, was isolated from the
rhizosphere of peanut plant and its salinity stress alleviation
ability was studied using tomato (Solanum lycopersicum
cv. Micro-Tom) plants. Based on 16S rDNA based phylogenetic
analysis, strain SK68 has been identified as a Streptomyces
sp. Strain SK68 had branched substrate mycelium bearing
smooth surfaced spores and the spore colour is brownish
grey on ISP4 medium. It exhibited enzyme activities such
as xylanase, cellulase, amylase, and pectinase and degraded
hypoxanthine, casein, and L-tyrosine. The strain SK68 differed
in its banding pattern in BOX-PCR and RAPD fingerprinting
compared to the closely matching type strains
Streptomyces erythrochromogenes NBRC 3304T (AB184746),
S. flavotricini NBRC 12770T (AB184132), S. racemochromogenes
NBRC 12906T (AB184235), and S. polychromogenes
NBRC 13072T (NR041109). Strain SK68 was evaluated for
its salinity stress-alleviating activity in tomato plants with
180 mmol/L NaCl under gnotobiotic condition. A significant
increase in plant biomass was observed in strain SK68-inoculated
tomato plants under salt stress compared to control
and salt-stressed non-inoculated plants.
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- Rapid Discrimination of Potato Scab-Causing Streptomyces Species Based on the RNase P RNA Gene Sequences
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Hang-Yeon Weon , Jaekyeong Song , Byung-Yong Kim , On-Suk Hur , In-Cheol Park , Joo-Won Suh
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J. Microbiol. 2011;49(5):791-796. Published online November 9, 2011
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DOI: https://doi.org/10.1007/s12275-011-1279-7
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743
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Scab disease significantly damages potatoes and other root crops. Some Streptomyces species have been reported as potato-scab pathogens. Identification of the phytopathogenic Streptomyces is mainly done on the basis of the 16S rRNA gene, but use of this gene has some limitations for discriminating these strains because they share high similarities of 16S rRNA gene sequences. We tested the RNase P RNA (rnpB) gene as a taxonomic marker to clarify the relationship among closely related scab-causing Streptomyces strains. The rnpB genes were analyzed for 41 strains including 9 isolates from Jeju, Korea. There were 4 highly variable regions including nucleotide gaps in the rnpB genes. Interspecies similarity of the rnpB gene in tested Streptomyces strains was lower than about 97%, while the intraspecies similarity was higher than about 98%. Phylogenetic analysis demonstrated that the rnpB tree has similar topology to the 16S rRNA gene tree, but produces a more divergent phyletic lineage. These results revealed that the rnpB gene could be used as a powerful taxonomic tool for rapid differentiation of closely related Streptomyces species. In addition, it was also suggested that the variable regions marked as α, β, γ, and δ in the rnpB gene could be useful markers for the detection of specific Streptomyces species.
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Chang-Gu Hyun , Sang-Suk Kim , Joo-Won Suh
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J. Microbiol. 2006;44(1):50-53.
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DOI: https://doi.org/2337 [pii]
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Abstract
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Cys-29 and Cys-251 of Streptomyces albus valine dehydrogenase (ValDH) were highly conserved
in the corresponding region of NAD(P)+-dependent amino acid dehydroganase sequences. To ascertain
the functional role of these cysteine residues in S. albus ValDH, site-directed mutagenesis
was performed to change each of the two residues to serine. Kinetic analyses of the enzymes mutated
at Cys-29 and Cys-251 revealed that these residues are involved in catalysis. We also constructed
mutant ValDH by substituting valine for leucine at 305 by site-directed mutagenesis. This
residue was chosen, because it has been proposed to be important for substrate discrimination by
phenylalanine dehydrogenase (PheDH) and leucine dehydrogenase (LeuDH). Kinetic anaysis of the
V305L mutant enzyme revealed that it is involved in the substrate binding site. However it displayed
less activity than the wild type enzyme toward all aliphatic and aromatic amino acids
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- Molecular Detection of [alpha]-Glucosidase Inhibitor-producing Actinomycetes
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Chang-Gu Hyun , Seung-Young Kim , Jin-Haeng Hur , Myung-Ji Seo , Joo-Won Suh , Soon-Ok Kim
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J. Microbiol. 2005;43(3):313-318.
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DOI: https://doi.org/2207 [pii]
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Abstract
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In this study, we demonstrate the use of a PCR-based method for the detection of the specific genes involved in natural-product biosynthesis. This method was applied, using specifically designed PCR primers, to the amplification of a gene segment encoding for sedo-heptulose 7-phosphate cyclase, which appears to be involved in the biosynthetic pathways of C_7N aminoacyclitol or its keto analogue-containing metabolites, in a variety of actinomycetes species. The sequences of DNA fragments (about 540 bp) obtained from three out of 39 actinomycete strains exhibited a high degree of homology with the sedo-heptulose 7-phosphate cyclase gene, which has been implicated in acarbose biosynthesis. The selective cultivation conditions of this experiment induced the expression of these loci, indicating that the range of C_7N aminoacyclitol or its keto analogue-group natural products might be far greater than was previously imagined. Considering that a total of approximately 20 C_7N aminoacyclitol metabolites, or its keto analogue-containing metabolites, have been described to date, it appears likely that some of the unknown loci described herein might constitute new classes of C_7N aminoacyclitol, or of its keto analogue-containing metabolites. As these metabolites, some of which contain valienamine, are among the most potent antidiabetic agents thus far discovered, the molecular detection of specific metabolite-producing actinomycetes may prove a crucial step in current attempts to expand the scope and diversity of natural-product discovery.
- Streptomyces griseus Trypsin (SGT) Has Gelatinase Activity and Its Proteolytic Activity Is Enhanced by Manganese
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Won-Jae Chi , Yoon-Hee Kim , Jong-Hee Kim , Dae-Kyung Kang , Sang-Soon Kang , Joo-Won Suh , Soon-Kwang Hong
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J. Microbiol. 2003;41(4):289-294.
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Abstract
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Gelatinase is a proteolytic enzyme that hydrolyzes gelatin. Gelatinolytic activity was detected from culture broths of Streptomyces griseus IFO13350 and HH1 by paper disc assays on 0.5% agar plates containing 1% gelatin. The concentrated extracellular protein from the S. griseus was analyzed by SDS polyacrylamide gel, and two proteins, with molecular weights of 30 and 28 kDa, respectively, were identified to have gelatinase activity by gelatin zymography. The protein with a molecular weight of 28 kDa was confirmed to be S. griseus trypsin (SGT). The effects of metal ions and metal chelators on the protease activity of the SGT were studied. Of the metal ions tested, only manganese was found to enhance the protease activity, 2.6 times, however, Co_2^+, Cu_2^+, and Zn_2^+, and metal chelators, such as EDTA and EGTA, inhibited the SGT activity. When the protease activity of the SGT was measured at various pHs, in the presence of 5 mM MnCl_2, its highest activity was at pH 11.0, whereas only 60% of the maximum activity was observed between pHs 4.0 and pH 6.0, and almost 80% activity between pHs 7.0 to pH 10.0. The protease activity was measured at various temperatures in the presence of 5 mM MnCl_2. The SGT was found to be stable up to 60℃ for 30 min, while only 16% of the enzyme activity remained at 60℃, and at 80℃ almost all the activity was lost. The optimal temperature for the protease activity was 50℃.
- Stable Secretion Vector Derived from the RCR (rolling-circle replication) Plasmid of Bacillus mesentericus
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Seung-Soo Lee , Jeong-Sun Han , In Hyung Lee , Young- Yel l Yang , Soon-Kwang Hong , Joo-Won Suh
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J. Microbiol. 2002;40(2):140-145.
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The 5.8 kb pMMH1, rolling-circle replication (RCR) plasmid of the wild type soil Bacillus mesentericus was developed into a novel secretion vector system in Bacillus subtilis. The pMMH1 turned out to have a replication origin and two open reading frames (ORFs) of the putative [gamma]-GTP and type I signal peptidase (sipP). To characterize the regions necessary for plasmid stability and high copy number, five vectors (pPS, pPP, pEN, pMN, pME) were constructed by disruption or deletion of each region in pMMH1. Like pMMH1, all constructed vectors were stable over 100 generations in a non-selective medium. Since pPS was the smallest (2.3 kb)of all, it was selected for the construction of a novel secretion vector. Using the [alpha]-amylase promoter/signal sequence of B. subtilils, the novel plasmid pJSN was constructed. When [beta]-glucosidase was expressed using pJSN, we found [beta]-glucosidase activity in the medium. This result strongly suggested that plasmid pJSN can be used for the production of bioactive peptides in B. subtilis.
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