The polyketide synthase OsPKS2 is essential for pollen exine and Ubisch body patterning in rice

作     者：Xiaolei Zhu Jing Yu Jianxin Shi Takayuki Tohge Alisdair R.Fernie Sagit Meir Asaph Aharoni Dawei Xu Dabing Zhang Wanqi Liang 

作者机构：Joint International Research Laboratory of Metabolic&Developmental SciencesShanghai Jiao Tong University-University of Adelaide Joint Centre for Agriculture and HealthSchool of Life Sciences and BiotechnologyShanghai Jiao Tong UniversityShanghai 200240China Central Metabolism GroupMax Planck Institute of Molecular Plant Physiology14476 Potsdam-GolmGermany Department of Plant SciencesWeizmann Institute of SciencePO Box 26Rehovot 76100Israel School of AgricultureFood and WineUniversity of AdelaideWaite CampusSA 5005Australia 

出 版 物：《Journal of Integrative Plant Biology》 (植物学报（英文版）)

年 卷 期：2017年第59卷第9期

页      面：612-628页

核心收录：

学科分类：09[农学] 0901[农学-作物学] 090102[农学-作物遗传育种] 

基　　金：supported by funds from the National Key Research and Development Program of China(No.2016YFD0101107) the National Key Basic Research Developments Program of the Ministry of Science and Technology of China(No.2013CB126902) the National Natural Science Foundation of China(No.31322040,31670309) the Innovative Research Team of the Ministry of Education and the 111 Project(No.B14016) 

主　　题：PKS The polyketide synthase OsPKS2 is essential for pollen exine and Ubisch body patterning in rice Figure 

摘      要：Lipid and phenolic metabolism are important for pollen exine formation. In Arabidopsis, polyketide synthases （PKSs） are essential for both sporopollenin biosynthesis and exine formation. Here, we characterized the role of a polyketide synthase （OsPKS2） in male reproduction of rice （Oryza sativa）. Recombinant OsPKS2 catalyzed the condensation of fatty acyl-CoA with malonyl- CoA to generate triketide and tetraketide α-pyrones, the main components of pollen exine. Indeed, the ospks2 mutant had defective exine patterning and was male sterile. However, the mutant showed no significant reduction in sporopollenin accumulation. Compared with the WT （wild type）, ospks2 displayed unconfined and amorphous tectum and nexine layers in the exine, and less organized Ubisch bodies. Like the pksb/lap5 mutant of the Arabidopsis ortholog, ospks2 showed broad alterations in the profiles of anther-related phenolic compounds. However, unlike pksb/laps, in which most detected phenolics were substantially decreased, ospks2 accumu- lated higher levels of phenolics. Based on these results and our observation that OsPKS2 is unable to fully restore the exine defects in the pksb/laps, we propose that PKS proteins have functionally diversified during evolution. Collectively, our results suggest that PKSs represent a conserved and diversified biochemical pathway for anther and pollen development in higher plants.