Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

文献类型： 外文期刊

第一作者： Jing, Hongwei

作者： Jing, Hongwei;Yang, Xiaolu;Zhang, Jian;Zheng, Huakun;Nian, Jinqiang;Feng, Jian;Li, Jiayang;Zuo, Jianru;Jing, Hongwei;Yang, Xiaolu;Zhang, Jian;Zheng, Huakun;Nian, Jinqiang;Feng, Jian;Li, Jiayang;Zuo, Jianru;Jing, Hongwei;Yang, Xiaolu;Zheng, Huakun;Liu, Xuehui;Dong, Guojun;Qian, Qian;Xia, Bin

作者机构：

关键词： LATERAL ROOT INITIATION;OF-FUNCTION MUTATION;BOX PROTEIN TIR1;PLANT DEVELOPMENT;ARABIDOPSIS;CYCLOPHILIN;GENE;RECEPTOR;DIAGEOTROPICA;PERCEPTION

期刊名称：NATURE COMMUNICATIONS （ 影响因子：14.919； 五年影响因子：15.805 ）

ISSN：

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收录情况： SCI

摘要： In plants, auxin signalling is initiated by the auxin-promoted interaction between the auxin receptor TIR1, an E3 ubiquitin ligase, and the Aux/IAA transcriptional repressors, which are subsequently degraded by the proteasome. Gain-of-function mutations in the highly conserved domain II of Aux/IAAs abolish the TIR1-Aux/IAA interaction and thus cause an auxin-resistant phenotype. Here we show that peptidyl-prolyl isomerization of rice OsIAA11 catalysed by LATERAL ROOTLESS2 (LRT2), a cyclophilin-type peptidyl-prolyl cis/trans isomerase, directly regulates the stability of OsIAA11. NMR spectroscopy reveals that LRT2 efficiently catalyses the cis/trans isomerization of OsIAA11. The lrt2 mutation reduces OsTIR1-OsIAA11 interaction and consequently causes the accumulation of a higher level of OsIAA11 protein. Moreover, knockdown of the OsIAA11 expression partially rescues the lrt2 mutant phenotype in lateral root development. Together, these results illustrate cyclophilin-catalysed peptidyl-prolyl isomerization promotes Aux/IAA degradation, as a mechanism regulating auxin signalling.

分类号： N

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