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Author Jing H., Yang X., Zhang J., Liu X., Zheng H., Dong G., Nian J., Feng J., Xia B., Qian Q., Li J., Zuo J.
Title Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling.
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 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.
Journal Nat Commun
Country China
Volume 6
Pages 7395
Year 2015
PubMed ID 26096057
PubMed Central ID -
DOI 10.1038/ncomms8395
URL -
Relation
Gene IAA11 IAA13 LRT2 TIR1
INSD -
Strain Wild Core Collection -
Induced Mutation Lines(NIG Collection) -
Sterile Seed Strain -
Lethal Embryo
Mutantion Strain
-
Stages in Each Organ
- Muant Lines (Gene)
-
Cultivated Varieties(NIG Collection) -
Stages in Each Organ -
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