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Cloning and characterization of a gene encoding ABP57, a soluble auxin-binding protein
Keunpyo Lee,Myung-Il Kim,Yu-Jihn Kwon,Minkyun Kim,김용삼,Donghern Kim 한국식물생명공학회 2009 Plant biotechnology reports Vol.3 No.4
Auxin-binding protein 57 (ABP57), a soluble auxin-binding protein, acts as a receptor to activate plasma membrane (PM) H?-ATPase. Here, we report the cloning of abp57 and the biochemical characterization of its protein expressed in E. coli. The analysis of internal amino acid sequences of ABP57 purified from rice shoots enabled us to search for the corresponding gene in protein DB of NCBI. Further BLAST analysis showed that rice has four abp57- like genes and maize has at least one homolog. Interestingly, Arabidopsis seems to have no homolog. Recombinant ABP57 expressed in E. coli caused the activation of PM H?-ATPase regardless of the existence of IAA. Scatchard analysis showed that the recombinant protein has relatively low affinity to IAA as compared to natural ABP57. These results collectively support the notion that the cloned gene is responsible for ABP57.
Antiviral Activity of a Type 1 Ribosome-inactivating Protein from Chenopodium album L.
Lee, Si-Myung,Cho, Kang-Jin,Kim, Yeong-Tae,Park, Hee-young,Kim, Su-il,Hwang, Young-Soo,Kim, Donghern 한국응용생명화학회 1999 Journal of Applied Biological Chemistry (J. Appl. Vol.42 No.4
The antiviral activity of CAP30 from Chenopodium album, a type1 ribosome-inactivating protein (RIP), was examined against 5 different plant viral pathogens, and its activity against Tobacco mosaic virus was compared to those of well known antiviral proteins such as Pokeweed Antiviral protein from leaves and seeds. When the inoculating concentration of Tobacco mosaic virus was varied from 0.4 to $400{\mu}g/ml$, it was observed that CAP30 at the concentration of $1{\mu}g/ml$ suppressed the viral infection of C. amaranthicolor and C. quinoa almost completely up to $40{\mu}g/ml$ Tobacco mosaic virus. Results from the assays for the inhibitions of in vitro translation of rabbit reticulocyte lysate and the suppression of Tobacco mosaic virus infection ($10{\mu}g/ml$) to C. quinoa indicated that CAP30 is a strong inhibitor of protein synthesis and virus infection. The infection of several viruses other than Tobacco mosaic virus to host plants were also inhibited by $5{\mu}g/ml$ CAP30, suggesting that a gene encoding CAP30 can be used to develop transgenic virus-resistant plants.