Proteins that interact with rice pumilio 1

Abstract

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