NIa-Pro of Papaya ringspot virus interacts with Carica papaya eukaryotic translation initiation factor 3 subunit G (CpeIF3G)

文献类型： 外文期刊

第一作者： Gao, Le

作者： Gao, Le;Tuo, Decai;Shen, Wentao;Yan, Pu;Li, Xiaoying;Zhou, Peng;Gao, Le;Tuo, Decai;Shen, Wentao;Yan, Pu;Li, Xiaoying;Zhou, Peng;Gao, Le

作者机构：

关键词： NIa-Pro;Eukaryotic translation initiation factor 3 subunit G;Papaya;PRSV;Protein-protein interaction

期刊名称：VIRUS GENES （ 影响因子：2.332； 五年影响因子：2.0 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： The interaction of papaya eukaryotic translation initiation factor 3 subunit G (CpeIF3G) with Papaya ringspot virus (PRSV) NIa-Pro was validated using a bimolecular fluorescence complementation assay in papaya protoplasts based on the previous yeast two-hybrid assay results. The C-terminal (residues 133-239) fragment of PRSV NIa-Pro and the central domain (residues 59-167) of CpeIF3G were required for effective interaction between NIa-Pro and CpeIF3G as shown by a Sos recruitment yeast two-hybrid system with several deletion mutants of NIa-Pro and CpeIF3G. The central domain of CpeIF3G, which contains a C2HC-type zinc finger motif, is required to bind to other eIFs of the translational machinery. In addition, quantitative real-time reverse transcription PCR assay confirmed that PRSV infection leads to a 2- to 4.5-fold up-regulation of CpeIF3G mRNA in papaya. Plant eIF3G is involved in various stress response by enhancing the translation of resistance-related proteins. It is proposed that the NIa-Pro-CpeIF3G interaction may impair translation preinitiation complex assembly of defense proteins and interfere with host defense.

分类号： R37

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