Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling
Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling
复制标题
肽基-脯氨酰异构化以水稻 Aux/IAA 为目标，在生长素信号传导过程中实现蛋白酶体降解
DOI：
10.1038/ncomms8395
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发表时间：
2015-06-01
影响因子：
16.6
通讯作者：
Zuo, Jianru
中科院分区：
文献类型：
--
作者：
Jing, Hongwei;Yang, Xiaolu;Zuo, Jianru
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-prolylcis/transisomerase, directly regulates the stability of OsIAA11. NMR spectroscopy reveals that LRT2 efficiently catalyses thecis/transisomerization of OsIAA11. Thelrt2mutation reduces OsTIR1–OsIAA11 interaction and consequently causes the accumulation of a higher level of OsIAA11 protein. Moreover, knockdown of theOsIAA11expression partially rescues thelrt2mutant phenotype in lateral root development. Together, these results illustrate cyclophilin-catalysed peptidyl-prolyl isomerization promotes Aux/IAA degradation, as a mechanism regulating auxin signalling.
