A potyvirus P1 protein interacts with the Rieske Fe/S protein of its host

文献类型： 外文期刊

第一作者： Shi, Yuhong

作者： Shi, Yuhong;Chen, Jiong;Hong, Xueyu;Chen, Jianping;Adams, Michael J.

作者机构：

期刊名称：MOLECULAR PLANT PATHOLOGY （ 影响因子：5.663； 五年影响因子：5.626 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： Yeast two-hybrid (Y2H) screens were used to test for interactions between the P1 protein of Soybean mosaic virus Pinellia isolate (SMV-P) and a cDNA expression library of its host, the aroid Pinellia ternata. Of the 13 independent interacting clones identified, ten were identical and had an open reading frame predicted to encode a 23.7-kDa protein closely related to the cytochrome b6/f complex Rieske Fe/S genes of plants. The interaction between SMV-P-P1 and the mature Rieske Fe/S protein (without transit peptide) of the host was confirmed by in vitro co-immunoprecipitation of the two proteins. Y2H assays using different parts of the two proteins showed that only the N-terminal part (amino acids 1-82) of SMV-P P1 was responsible for the interaction with the Rieske Fe/S protein and that amino acids 1-33 interacted only with the transit peptide, while amino acids 34-82 could interact with the entire Rieske Fe/S protein. SMV-P P1 also interacted moderately with the Rieske Fe/S protein of its other hosts, soybean and Zantedeschia aethiopica, but weakly with that of the non-host Arabidopsis thaliana. The P1-Rieske Fe/S protein interactions are likely to be involved in symptom development, and the very variable N-terminus of P1 may play an important role in host adaptation.

分类号： Q94

  • 相关文献
作者其他论文 更多>>

微信小程序