Purification and characterization of a new ribosome inactivating protein from cinchonaglycoside C-treated tobacco leaves
文献类型: 外文期刊
作者: Li, Yanmei 1 ; Jia, Yantao 2 ; Zhang, Zhongkai 2 ; Chen, Xiaoying 3 ; He, Hongping; Fang, Rongxiang; Hao, Xiaoji 1 ;
作者机构: 1.Chinese Acad Sci, Inst Microbiol, State Key Lab Plant Genom, Beijing 100080, Peoples R China
2.Chinese Acad Sci, Inst Microbiol, State Key Lab Plant Genom, Beijing 100080, Peoples R China; Chinese Acad Sci, Kunming Inst Bot, State Key Lab Photochem & Plant Resources W China, Kunming 650204, Peoples R China; Yunnan Acad Agr Sci, Lab Plant Virol, Kunming 650223, Peoples R China; Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
3.Chinese Acad Sci, Inst Microbiol, State Key Lab Plant Genom, Beijing 100080, Peoples R China; Chinese Acad Sci, Kunming Inst Bot, State Key Lab Photochem & Plant Resources W China, Kunming 650204, Peoples R China; Yunnan Acad Agr Sci, Lab
关键词: antiviral protein;Cinchonaglycoside C (1);coat protein;medical plant;ribosome inactivating protein;salicylic acid;tobacco mosaic virus
期刊名称:JOURNAL OF INTEGRATIVE PLANT BIOLOGY ( 影响因子:7.061; 五年影响因子:6.002 )
ISSN: 1672-9072
年卷期: 2007 年 49 卷 9 期
页码:
收录情况: SCI
摘要: A new ribosome-in activating protein (RIP) with a molecular weight of 31 kDa induced by Cinchonaglycoside C (1) designated CIP31, was isolated from tobacco leaves. Analysis of this protein sequence indicated that it belongs to the RIP family and it was distinct from the other plant RIPs reported previously at its N-terminal amino acid sequence. CIP31 can directly impair synthesis of coat protein (CP) of tobacco mosaic virus JMV), which resulted in inhibition of TMV long distance movement and multiplication in tobacco plants at concentrations of ng/mL. Furthermore, no toxicity was shown to the growth and fertility of the plants. CIP31 was synthesized only in the presence of Cinchonaglycoside C (1) and was independent of the salicylic acid (SA) signal pathway. We provided evidence for the SA-independent biological induction of resistance.
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