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- [Minireview]Cytoplasmic molecular chaperones in Pseudomonas species
- Hyunhee Kim , Seongjoon Moon , Soojeong Ham , Kihyun Lee , Ute Römling , Changhan Lee
- J. Microbiol. 2022;60(11):1049-1060. Published online November 1, 2022
- DOI: https://doi.org/10.1007/s12275-022-2425-0
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Abstract
- Pseudomonas is widespread in various environmental and host niches. To promote rejuvenation, cellular protein homeostasis must be finely tuned in response to diverse stresses, such as extremely high and low temperatures, oxidative stress, and desiccation, which can result in protein homeostasis imbalance. Molecular chaperones function as key components that aid protein folding and prevent protein denaturation. Pseudomonas, an ecologically important bacterial genus, includes human and plant pathogens as well as growth-promoting symbionts and species useful for bioremediation. In this review, we focus on protein quality control systems, particularly molecular chaperones, in ecologically diverse species of Pseudomonas, including the opportunistic human pathogen Pseudomonas aeruginosa, the plant pathogen Pseudomonas syringae, the soil species Pseudomonas putida, and the psychrophilic Pseudomonas antarctica.
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- An innovative utilization approach for by-products of biogas desulfurization：Co-hydrothermal treatment of sulfur with biogas slurry to prepare sulfur-enriched liquid fertilizer
Zhijie Xie, Fang Deng, Yuqin Wan, Yiping Luo, Qin Cao, Yichao Chen, Dong Li
Process Biochemistry.2024; 147: 522. CrossRef - Isolation of Pseudomonas oleovorans Carrying Multidrug Resistance Proteins MdtA and MdtB from Wastewater
Haifeng Wang, Chenyang Sun, Xing Chen, Kai Yan, Hongxuan He
Molecules.2023; 28(14): 5403. CrossRef -
Development of heat-shock resistance in
Legionella pneumophila
modeled by experimental evolution
Jeffrey Liang, Gillian Cameron, Sébastien P. Faucher, Christopher A. Elkins
Applied and Environmental Microbiology.2023;[Epub] CrossRef
- An innovative utilization approach for by-products of biogas desulfurization：Co-hydrothermal treatment of sulfur with biogas slurry to prepare sulfur-enriched liquid fertilizer
Research Support, Non-U.S. Gov't
- Molecular Cloning and Characterization of a Large Subunit of Salmonella typhimurium Glutamate Synthase (GOGAT) Gene in Escherichia coli
- 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
- J. Microbiol. 2006;44(3):301-310.
- DOI: https://doi.org/2382 [pii]
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Abstract
- 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%.
- Molecular cloning of the arginine biosynthetic genes from corynebacterium glutamicum
- Chun, Jae Yeon , Jung, Sam Il , Ko, Soon Young , Park, Mee Young , Kim, Soo Young , Lee, Heung Shickc , Cheon, Choong Ill , Min, Kyung Hee , Lee, Myeong Sok
- J. Microbiol. 1996;34(4):355-362.
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Abstract
- Complementation cloning of the argC, E, B D, F, and G genes in Corynebacterium glutamicum was done by transforming the genomic DNA library into the corresponding arginine auxotrophs fo Escherichia coli. Recombinant plasmids containing 6.7 kb and 4.8kb fragments complementing the E. coli arg B mutant were also able to complement the E. coli argC, E, A, D, and F mutants, indicating the clustered organization of the arginine biosynthetic genes within the cloned DNA fragments. The insert DNA fragments in the recombinant plasmids, named pRB1 AND pRB2, were physically mapped with several restriction enzymes. By further subcloning the entire DNA fragment containing the functions and by complementation analysis, we located the arg genes in the order of ACEBDF on the restriction map. We also determined the DNA nucleotide sequence of the fragment and report here the sequence of the argB gene. When compared to that with the nutant strain, higherh enzyme activity of N-acetylglutamate kinase was detacted in the extract of the mutant carrying the plasmid containing the putative argB gene, indicating that the plasmid contains a functional argB gene. Deduced amino acid sequence of the argB gene shows45%, 38%, and 25% identity to that from Bacillus strearothermophilus, Bacillus substilus, and E. coli respectively. Our long term goal is genetically engineering C. glutamicum which produces more arginine than a wild type strain does.
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