Research articles
ScienceAsia 39 (2013): 615-619 |doi:
10.2306/scienceasia1513-1874.2013.39.615
Proteins that interact with rice pumilio 1
Yuyun Sugihartia, Aqil Azizib, Mukhamad Su'udia,c,*
ABSTRACT: The N-terminal region of rice pumilio 1 fused with the binding domain (BD-OsPUM1) was used as a bait construct in yeast two-hybrid screening with a rice cDNA library as prey. Several interacting proteins were screened in a stringent media and tested with beta-galactose filter assay. The nucleotide sequences encoding interacting proteins were determined and annotated according to the rice genome database. These proteins are sigma factor F inhibitor, RPL18C, RUBQ2, RPL24A, RCY1, small nuclear ribonucleoprotein G, transferase hexapeptide repeat-containing protein, dormancy-associated protein, and putative expressed proteins with the accessions NP_001067038 and EEE55952. This study suggested that OsPUM1 protein is associated with several biological processes involved in morphology determination, protein folding and plant immunity.
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| a |
Department of Integrative Plant Science, Chung-Ang University, Anseong 456-756, Korea |
| b |
Department of Marine Biotechnology, University of Science and Technology, Daejeon 305-333, Korea |
| c |
Department of Agricultural Biotechnology, National Academy of Agricultural Science, RDA, Suwon 441-707, Korea |
* Corresponding author, E-mail: msuudi.rda@gmail.com
Received 5 Nov 2012, Accepted 4 Aug 2013
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