Survey of rice proteins interacting with OsFCA and OsFY proteins which are homologous to the arabidopsis flowering time proteins, FCA and FY

• Published in: Plant and cell physiology Vol. 50; no. 8; pp. 1479 - 1492
• Main Authors: Jang, Y.H.(Korea Univ., Seoul (Korea R.)), Park, H.Y, Kim, S.K, Lee, J.H, Suh, M.C, Chung, Y.S, Paek, K.H, Kim, J.K
• Format: Journal Article
• Language: English
• Published: Japan Oxford University Press 01.08.2009; Oxford Publishing Limited (England)
• Subjects: Amino Acid Sequence; ARABIDOPSIS; FLORACION; FLORAISON; FLOWERING; Flowering time; Flowers - genetics; Flowers - metabolism; GENE; Gene Expression Regulation, Plant; GENES; Molecular Sequence Data; mRNA Cleavage and Polyadenylation Factors - genetics; mRNA Cleavage and Polyadenylation Factors - metabolism; Oryza - genetics; Oryza - metabolism; ORYZA SATIVA; OsFCA; OsFY; Plant Proteins - genetics; Plant Proteins - metabolism; Polyadenylation; Protein Binding; Protein interaction; Protein Interaction Mapping; PROTEINAS; PROTEINE; PROTEINS; Rice; RNA, Plant - genetics; RNA-Binding Proteins - genetics; RNA-Binding Proteins - metabolism; Two-Hybrid System Techniques; OsFY; Flowering time; Protein interaction; OsFCA; Polyadenylation; Rice
• ISSN: 0032-0781; 1471-9053
• DOI: 10.1093/pcp/pcp093

The FCA protein is involved in controlling flowering time and plays more general roles in RNA-mediated chromatin silencing in Arabidopsis. It contains two RNA-binding domains and a WW domain. The FCA protein interacts with FY, a polyadenylation factor, via its WW domain. We previously characterized a rice gene, OsFCA, which was homologous to FCA. Here, we found that the OsFCA protein could interact through its WW domain with the following proteins: OsFY, a protein containing a CID domain present in RNA-processing factors such as Pcf11 and Nrd1; a protein similar to splicing factor SF1; a protein similar to FUSE splicing factor; and OsMADS8. The FY protein is associated with the 3′ end processing machinery in Arabidopsis. Thus, we examined interactions between OsFY and the rice homologs (OsCstF-50, -64 and -77) of the AtCstF-50, -64 and -77 proteins. We found that OsFY could bind OsCstF50, whereas the OsCstF77 protein could bridge the interaction between OsCstF50 and OsCstF64. Taken together, our data suggest that OsFCA could interact with several proteins other than OsFY through its WW domain and may play several roles in rice.