Premium
OsMADS32 interacts with PI‐like proteins and regulates rice flower development
Author(s) -
Wang Huanhuan,
Zhang Liang,
Cai Qiang,
Hu Yun,
Jin Zhenming,
Zhao Xiangxiang,
Fan Wei,
Huang Qianming,
Luo Zhijing,
Chen Mingjiao,
Zhang Dabing,
Yuan Zheng
Publication year - 2015
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/jipb.12248
Subject(s) - mutant , complementation , bimolecular fluorescence complementation , biology , stamen , meristem , gene , protein fragment complementation assay , phenotype , genetics , amino acid , protein domain , microbiology and biotechnology , botany , pollen
OsMADS32 is a monocot specific MIKC c 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.