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Sohn H.,South Korean National Institute of Crop Science | Cho K.,South Korean National Institute of Crop Science | Cho J.,South Korean National Institute of Crop Science | Gwon O.,South Korean National Institute of Crop Science | And 4 more authors.
Journal of Plant Biotechnology | Year: 2014

We performed in vitro assay and field trials to assess levels of changes in intrinsic properties and resistance against soft rot of the potato cv. Dejima upon the introduction of a soybean calmodulin 4 gene (SCaM4). Field trials with four lines overexpressing SCaM4 gene were conducted over two seasons, and harvested tubers were evaluated in bioassay for resistance to Pectobact erium carotovorum ssp. carot ovorum. The SCaM4 transgenic potato lines inoculated with 108 CFU/ml of P. carotovorum ssp. carotovorum showed enhanced resistance compared to control. Among the SCaM4 transgenic lines, the transgenic line SCaM4-4 exhibited the highest tolerance to soft rot in vitro assays, so did in field trials. In the field trial, the soft rot resistance of SCaM4-4 line was more than 5 times higher compared to that of control cultivar, Dejima. The major agronomic characteristics of the SCaM4 transgenic lines were not different from those of the nontransgenic 'Dejima'. The result demonstrated that the transformation of a calmodulin 4 gene was a successful strategy in development of potato cultivar enhanced to soft rot. © Korean Society for Plant Biotechnology. Source


Park H.C.,Plant Molecular Biology and Biotechnology Research Center | Park H.C.,Gyeongsang National University | Park C.Y.,Plant Molecular Biology and Biotechnology Research Center | Koo S.C.,Plant Molecular Biology and Biotechnology Research Center | And 12 more authors.
Plant Cell Reports | Year: 2010

Plants express many calmodulins (CaMs) and calmodulin-like (CML) proteins that sense and transduce different Ca2+ signals. Previously, we reported divergent soybean (Glycine max) CaM isoforms (GmCaM4/5) with differential abilities to activate CaM-dependent enzymes. To elucidate biological functions of divergent CaM proteins, we isolated a cDNA encoding a CML protein, AtCML8, from Arabidopsis. AtCML8 shows highest identity with GmCaM4 at the protein sequence level. Expression of AtCML8 was high in roots, leaves, and flowers but low in stems. In addition, the expression of AtCML8 was induced by exposure to salicylic acid or NaCl. AtCML8 showed typical characteristics of CaM such as Ca2+-dependent electrophoretic mobility shift and Ca2+ binding ability. In immunoblot analyses, AtCML8 was recognized only by antiserum against GmCaM4 but not by GmCaM1 antibodies. Interestingly, AtCML8 was able to activate phosphodiesterase (PDE) but did not activate NAD kinase. These results suggest that AtCML8 acts as a CML protein in Arabidopsis with characteristics similar to soybean divergent GmCaM4 at the biochemical levels. © 2010 Springer-Verlag. Source

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