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Plant and Cell Physiology Advance Access published online on June 26, 2009
Plant and Cell Physiology, doi:10.1093/pcp/pcp093
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org

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

Yun Hee Jang1, Hyo-Young Park1, Soon-Kap Kim1, Jeong Hwan Lee1, Mi Chung Suh2, Young Soo Chung3, Kyung-Hee Paek1 and Jeong-Kook Kim1,*

1Plant Signaling Network Research Center, School of Life Sciences and Biotechnology, Korea University, Seoul, 136-701, Korea
2Department of Plant Biotechnology and Agricultural Plant Stress Research Center, College of Agriculture and Life Sciences, Chonnam National University, Gwangju, 500-757, Korea
3Life Science and Natural Resources, Dong-A University, 840 Hadan-dong, Busan 604-714, Korea

*Corresponding author: Prof. Jeong-Kook Kim, Plant Signaling Network Research Center, School of Life Sciences and Biotechnology, Korea University, 5-1 Anam-Dong, Seongbuk-Ku, Seoul 136-701, Korea, Tel: +82-2-3290-3157, Fax: +82-2-927-9028, e-mail; jkkim{at}korea.ac.kr


  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 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 the OsFY and the rice homologs (OsCstF-50, -64, -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.

Keywords: flowering time - OsFCA - OsFY - polyadenylation - protein interaction - rice

(Received April 15, 2009; Accepted June 23, 2009)
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