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.