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Survey of rice proteins interacting with OsFCA and OsFY proteins which are homologous to the Arabidopsis flowering time proteins, FCA and FY.
Jang, Yun Hee; Park, Hyo-Young; Kim, Soon-Kap; Lee, Jeong Hwan; Suh, Mi Chung; Chung, Young Soo; Paek, Kyung-Hee; Kim, Jeong-Kook.
Afiliación
  • Jang YH; Plant Signaling Network Research Center, School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Korea.
Plant Cell Physiol ; 50(8): 1479-92, 2009 Aug.
Article en En | MEDLINE | ID: mdl-19561057
ABSTRACT
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.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas de Plantas / Oryza / Proteínas de Unión al ARN / Factores de Escisión y Poliadenilación de ARNm Idioma: En Revista: Plant Cell Physiol Asunto de la revista: BOTANICA Año: 2009 Tipo del documento: Article

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas de Plantas / Oryza / Proteínas de Unión al ARN / Factores de Escisión y Poliadenilación de ARNm Idioma: En Revista: Plant Cell Physiol Asunto de la revista: BOTANICA Año: 2009 Tipo del documento: Article