Purification and Characterization of a New Ribosome Inactivating Protein from Cinchonaglycoside C-tr

来源 :Journal of Integrative Plant Biology | 被引量 : 0次 | 上传用户:sunrain0428
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A new ribosome-inactivating protein(RIP)with a molecular weight of 31 kDa induced by Cinchonaglycoside C(1)designatedCLP31,was isolated from tobacco leaves.Analysis of this protein sequence indicated that it belongs to the RIP family and itwas distinct from the other plant RIPs reported previously at its N-terminal amino acid sequence.CIP31 can directly impairsynthesis of coat protein(CP)of tobacco mosaic virus(TMV),which resulted in inhibition of TMV long distance movementand multiplication in tobacco plants at concentrations of ng/mL.Furthermore,no toxicity was shown to the growth andfertility of the plants.CIP31 was synthesized only in the presence of Cinchonaglycoside C(1)and was independent of thesalicylic acid(SA)signal pathway.We provided evidence for the SA-independent biological induction of resistance. A new ribosome-inactivating protein (RIP) with a molecular weight of 31 kDa induced by Cinchonaglycoside C (1) designated CLP31, was isolated from tobacco leaves. Analysis of this protein sequence indicated that it belongs to the RIP family and itwas distinct from the other plant RIPs reported previously at its N-terminal amino acid sequence. CIP31 can directly impairsynthesis 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.
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