J Integr Plant Biol. ›› 2015, Vol. 57 ›› Issue (5): 504-513.DOI: 10.1111/jipb.12248

Special Issue: Rice Genomics and Agriculture

• Plant Reproduction Biology • Previous Articles    

OsMADS32 interacts with PI-like proteins and regulates rice flower development

Huanhuan Wang1†, Liang Zhang1,2†, Qiang Cai1†, Yun Hu1, Zhenming Jin1, Xiangxiang Zhao3, Wei Fan1, Qianming Huang2, Zhijing Luo1, Mingjiao Chen1, Dabing Zhang1 and Zheng Yuan1*   

  1. 1State Key Laboratory of Hybrid Rice, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China
    2College of Life and Basic Sciences, Sichuan Agricultural University, Sichuan, China
    3Jiangsu Key Laboratory for Eco-Agricultural Biotechnology around Hongze Lake, Huaiyin Normal University, Huaian, China
  • Received:2014-04-29 Accepted:2014-07-29 Published:2014-08-01
  • About author:These authors contribute equally to this work.
    *Correspondence: E-mail: zyuan@sjtu.edu.cn

Abstract:

OsMADS32 is a monocot specific MIKCc type MADS-box gene that plays an important role in regulating rice floral meristem and organs identity, a crucial process for reproductive success and rice yield. However, its underlying mechanism of action remains to be clarified. Here, we characterized a hypomorphic mutant allele of OsMADS32/CFO1, cfo1-3 and identified its function in controlling rice flower development by bioinformatics and protein-protein interaction analysis. The cfo1-3 mutant produces defective flowers, including loss of lodicule identity, formation of ectopic lodicule or hull-like organs and decreased stamen number, mimicking phenotypes related to the mutation of B class genes. Molecular characterization indicated that mis-splicing of OsMADS32 transcripts in the cfo1-3 mutant resulted in an extra eight amino acids in the K-domain of OsMADS32 protein. By yeast two hybrid and bimolecular fluorescence complementation assays, we revealed that the insertion of eight amino acids or deletion of the internal region in the K1 subdomain of OsMADS32 affects the interaction between OsMADS32 with PISTILLATA (PI)-like proteins OsMADS2 and OsMADS4. This work provides new insight into the mechanism by which OsMADS32 regulates rice lodicule and stamen identity, by interaction with two PI-like proteins via its K domain.

 

Wang H, Zhang L, Cai Q, Hu Y, Jin Z, Zhao X, Fan W, Huang Q, Luo Z, Chen M, Zhang D, Yuan Z (2015) OsMADS32 interacts with PI‐like proteins and regulates rice flower development. J Integr Plant Biol 57:
504–513. doi: 10.1111/jipb.12248

Key words: Floral organ identity, hypomorphic mutant, K domain, OsMADS32, protein interaction

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