• Title/Summary/Keyword: cellulose synthase

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Identification of Plant Factors Involving in Agrobacterium-mediated Plant Transformation

  • Nam, Jaesung
    • Korean Journal of Plant Tissue Culture
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    • v.27 no.5
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    • pp.387-393
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    • 2000
  • The process by which Agrobacterium tumefaciens genetically transforms plants involves a complex series of reactions communicated between the pathogen and the plants. To identify plant factors involved in agrobacterium-mediated plant transformation, a large number of T-DNA inserted Arabidopsis thaliana mutant lines were investigated for susceptibility to Agrobacterium infection by using an in vitro root inoculation assay. Based on the phenotype of tumorigenesis, twelve T-DNA inserted Arabidopsis mutants(rat) that were resistant to Agrobacterium transformation were found. Three mutants, rat1, rat3, and rat4 were characterized in detail. They showed low transient GUS activity and very low stable transformation efficiency compared to the wild-type plant. The resistance phenotype of rat1 and rats resulted from decreased attachment of Agrobacterium tumefaciens to inoculated root explants. They may be deficient in plant actors that are necessary for bacterial attachment to plant cells. The disrupted genes in rat1, rat3, and rat4 mutants were coding a arabinogalactan protein, a likely cell wall protein and a cellulose synthase-like protein, respectively.

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Identification of Protein Arginine Methyltransferase 5 as a Regulator for Encystation of Acanthamoeba

  • Moon, Eun-Kyung;Hong, Yeonchul;Chung, Dong-Il;Goo, Youn-Kyoung;Kong, Hyun-Hee
    • Parasites, Hosts and Diseases
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    • v.54 no.2
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    • pp.133-138
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    • 2016
  • Encystation is an essential process for Acanthamoeba survival under nutrient-limiting conditions and exposure to drugs. The expression of several genes has been observed to increase or decrease during encystation. Epigenetic processes involved in regulation of gene expression have been shown to play a role in several pathogenic parasites. In the present study, we identified the protein arginine methyltransferase 5 (PRMT5), a known epigenetic regulator, in Acanthamoeba castellanii. PRMT5 of A. castellanii (AcPRMT5) contained domains found in S-adenosylmethionine-dependent methyltransferases and in PRMT5 arginine-N-methyltransferase. Expression levels of AcPRMT5 were increased during encystation of A. castellanii. The EGFP-PRMT5 fusion protein was mainly localized in the nucleus of trophozoites. A. castellanii transfected with siRNA designed against AcPRMT5 failed to form mature cysts. The findings of this study lead to a better understanding of epigenetic mechanisms behind the regulation of encystation in cyst-forming pathogenic protozoa.

Metagenomic and Proteomic Analyses of a Mangrove Microbial Community Following Green Macroalgae Enteromorpha prolifera Degradation

  • Wu, Yijing;Zhao, Chao;Xiao, Zheng;Lin, Hetong;Ruan, Lingwei;Liu, Bin
    • Journal of Microbiology and Biotechnology
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    • v.26 no.12
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    • pp.2127-2137
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    • 2016
  • A mangrove microbial community was analyzed at the gene and protein levels using metagenomic and proteomic methods with the green macroalgae Enteromorpha prolifera as the substrate. Total DNA was sequenced on the Illumina HiSeq 2000 PE-100 platform. Two-dimensional gel electrophoresis in combination with liquid chromatography tandem mass spectrometry was used for proteomic analysis. The metagenomic data revealed that the orders Pseudomonadales, Rhizobiales, and Sphingomonadales were the most prevalent in the mangrove microbial community. By monitoring changes at the functional level, proteomic analyses detected ATP synthase and transporter proteins, which were expressed mainly by members of the phyla Proteobacteria and Bacteroidetes. Members of the phylum Proteobacteria expressed a high number of sugar transporters and demonstrated specialized and efficient digestion of various glycans. A few glycoside hydrolases were detected in members of the phylum Firmicutes, which appeared to be the main cellulose-degrading bacteria. This is the first report of multiple "omics" analysis of E. prolifera degradation. These results support the fact that key enzymes of glycoside hydrolase family were expressed in large quantities, indicating the high metabolic activity of the community.

The Effect of Oryzalin on Growth and Gravitropism in Arabidopsis Roots (Oryzalin이 애기장대 뿌리 생장과 굴중성 반응에 미치는 작용)

  • Go, Jin Gyu;Park, Sun Ill;Kim, Soon Young
    • Journal of Life Science
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    • v.31 no.2
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    • pp.109-114
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    • 2021
  • Oryzalin is a dinitroaniline herbicide that has been known to disrupt microtubules. Microtubules and microfilaments are components of cytoskeletons that are implicated in plant cell growth, which requires the synthesis of cellulose when cell walls elongate. In addition, microtubules are also involved in the sedimentation of statoliths, which regulate the perception of gravity in the columella cells of root tips. In this study, we investigated the effect of oryzalin on the growth and gravitropic response of Arabidopsis roots. The role of ethylene in oryzalin's effect was also examined using these roots. Treatment of oryzalin at a concentration of 10-4 M completely inhibited the roots' growth and gravitropic response. At a concentration of 10-6 M oryzalin, root growth was inhibited by 47% at 8 hr when compared to control. Gravitropic response was inhibited by about 38% compared to control in roots treated with 10-6 M oryzalin for 4 hr. To understand the role of oryzalin in the regulation of root growth and gravitropic response, we measured ethylene production in root segments treated with oryzalin. It was found that the addition of oryzalin stimulated ethylene production through the activation of ACC oxidase and ACC synthase genes, which are key components in the synthesis of ethylene. From these findings, it can be inferred that oryzalin inhibits the growth and gravitropic response of Arabidopsis roots by stimulating ethylene production. The increased ethylene alters the arrangement of the microtubules, which eventually interferes with the growth of the cell wall.