Shaohua Xu, Zhibin Zhang, Beibei Jing, Patrick Gannon, Jinmei Ding, Fang Xu, Xin Li, Yuelin Zhang
Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, China.
PLoS genetics 2011 JunTransportin-SR (TRN-SR) is a member of the importin-β super-family that functions as the nuclear import receptor for serine-arginine rich (SR) proteins, which play diverse roles in RNA metabolism. Here we report the identification and cloning of mos14 (modifier of snc1-1, 14), a mutation that suppresses the immune responses conditioned by the auto-activated Resistance (R) protein snc1 (suppressor of npr1-1, constitutive 1). MOS14 encodes a nuclear protein with high similarity to previously characterized TRN-SR proteins in animals. Yeast two-hybrid assays showed that MOS14 interacts with AtRAN1 via its N-terminus and SR proteins via its C-terminus. In mos14-1, localization of several SR proteins to the nucleus was impaired, confirming that MOS14 functions as a TRN-SR. The mos14-1 mutation results in altered splicing patterns of SNC1 and another R gene RPS4 and compromised resistance mediated by snc1 and RPS4, suggesting that nuclear import of SR proteins by MOS14 is required for proper splicing of these two R genes and is important for their functions in plant immunity.
Shaohua Xu, Zhibin Zhang, Beibei Jing, Patrick Gannon, Jinmei Ding, Fang Xu, Xin Li, Yuelin Zhang. Transportin-SR is required for proper splicing of resistance genes and plant immunity. PLoS genetics. 2011 Jun;7(6):e1002159
PMID: 21738492
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