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Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling
Hongwei Jing,Xiaolu Yang,Jian Zhang,Xuehui Liu,Huakun Zheng,Guojun Dong,Jinqiang Nian,Jian Feng,Bin Xia,Qian Qian,Jiayang Li & Jianru Zuo
NATURE COMMUNICATIONS
Abstract
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 OsIAA11expression 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.
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论文编号: |
DOI:10.1038/ncomms8395 |
论文题目: |
Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling |
英文论文题目: |
Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling |
第一作者: |
Hongwei Jing,Xiaolu Yang,Jian Zhang,Xuehui Liu,Huakun Zheng,Guojun Dong,Jinqiang Nian,Jian Feng,Bin Xia,Qian Qian,Jiayang Li & Jianru Zuo |
英文第一作者: |
Hongwei Jing,Xiaolu Yang,Jian Zhang,Xuehui Liu,Huakun Zheng,Guojun Dong,Jinqiang Nian,Jian Feng,Bin Xia,Qian Qian,Jiayang Li & Jianru Zuo |
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2015-06-22 |
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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 OsIAA11expression 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. |
英文摘要: |
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 OsIAA11expression 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. |
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NATURE COMMUNICATIONS |
英文刊物名称: |
NATURE COMMUNICATIONS |
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其它备注: |
Hongwei Jing,Xiaolu Yang,Jian Zhang,Xuehui Liu,Huakun Zheng,Guojun Dong,Jinqiang Nian,Jian Feng,Bin Xia,Qian Qian,Jiayang Li & Jianru Zuo. Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling. NATURE COMMUNICATIONS. DOI:10.1038/ncomms8395 |
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