- Gibberellin-Producing Promicromonospora sp. SE188 Improves Solanum lycopersicum Plant Growth and Influences Endogenous Plant Hormones
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Sang-Mo Kang , Abdul Latif Khan , Muhammad Hamayun , Javid Hussain , Gil-Jae Joo , Young-Hyun You , Jong-Guk Kim , In-Jung Lee
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J. Microbiol. 2012;50(6):902-909. Published online December 30, 2012
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DOI: https://doi.org/10.1007/s12275-012-2273-4
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Plant growth-promoting rhizobacteria (PGPR) producing gibberellins (GAs) can be beneficial to plant growth and development. In the present study, we isolated and screened a new strain of Promicromonospora sp., SE188, isolated from soil. Promicromonospora sp. SE188 secreted GAs into its growth medium and exhibited phosphate solubilization potential. The PGPR produced physiologically active (GA1 and GA4) and inactive (GA9, GA12, GA19, GA20, GA24, GA34, and GA53) GAs in various quantities detected by GC/MS-SIM. Solanum lycopersicum (tomato) plants inoculated with Promicromonospora sp. SE188 showed a significantly higher
shoot length and biomass as compared to controls where PGPR-free nutrient broth (NB) and distilled water (DW) were applied to plants. The presence of Promicromonospora sp. SE188 significantly up-regulated the non C-13 hydroxylation
GA biosynthesis pathway (GA12→GA24→GA9→GA4→GA34) in the tomato plants as compared to the NB and DW control plants. Abscisic acid, a plant stress hormone, was significantly down-regulated in the presence of Promicromonospora sp. SE188. Contrarily, salicylic acid was significantly higher in the tomato plant after Promicromonospora sp. SE188 inoculation as compared to the controls. Promicromonospora sp. SE188 showed promising stimulation of tomato plant growth. From the results it appears that Promicromonospora sp. SE188 has potential as a bio-fertilizer and should be more broadly tested in field trials for higher crop production in eco-friendly farming systems.
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- Molecular Cloning and Characterization of a Large Subunit of Salmonella typhimurium Glutamate Synthase (GOGAT) Gene in Escherichia coli
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Tae-Wook Chung , Dong-Ick Lee , Dong-Soo Kim , Un-Ho Jin , Chun Park , Jong-Guk Kim , Min-Gon Kim , Sang-Do Ha , Keun-Sung Kim , Kyu-Ho Lee , Kwang-Yup Kim , Duck Hwa Chung , Cheorl-Ho Kim
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J. Microbiol. 2006;44(3):301-310.
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DOI: https://doi.org/2382 [pii]
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Abstract
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Two pathways of ammonium assimilation and glutamate biosynthesis have been identified in microorganisms. One pathway involves the NADP-linked glutamate dehydrogenase, which catalyzes the amination of 2-oxoglutarate to form glutamate. An alternative pathway involves the combined activities of glutamine synthetase, which aminates glutamate to form glutamine, and glutamate synthase, which transfers the amide group of glutamine to 2-oxoglutarate to yield two molecules of glutamate. We have cloned the large subunit of the glutamate synthase (GOGAT) from Salmonella typhimurium by screening the expression of GOGAT and complementing the gene in E. coli GOGAT large subunit-deficient mutants. Three positive clones (named pUC19C12, pUC19C13 and pUC19C15) contained identical
<br>Sau3AI fragments, as determined by restriction mapping and Southern hybridization, and expressed GOGAT efficiently and constitutively using its own promoter in the heterologous host. The coding region expressed in Escherichia coli was about 170 kDa on SDS-PAGE. This gene spans 4,732 bases, contains an open reading frame of 4,458 nucleotides, and encodes a mature protein of 1,486 amino acid residues (Mr = 166,208). The FMN-binding domain of GOGAT contains 12 glycine residues, and the 3Fe-4S cluster has 3 cysteine residues. The comparison of the translated amino acid sequence of the Salmonella GOGAT with sequences from other bacteria such as Escherichia coli, Salmonella enterica, Shigella flexneri, Yersinia pestis, Vibrio vulnificus and Pseudomonas aeruginosa shows sequence identity between 87 and 95%.
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