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Purification and Characterization of a New Ribosome Inactivating Protein from Cinchonaglycoside C‐treated Tobacco Leaves
Author(s) -
Li Yanmei,
Jia Yantao,
Zhang Zhongkai,
Chen Xiaoying,
He Hongping,
Fang Rongxiang,
Hao Xiaojiang
Publication year - 2007
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/j.1744-7909.2007.00476.x
Subject(s) - tobacco mosaic virus , salicylic acid , ribosome inactivating protein , coat protein , biology , protein biosynthesis , biochemistry , ribosome , chemistry , botany , virus , rna , virology , gene
A new ribosome‐inactivating 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 (TMV), 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.