Sclerotinia sclerotiorum (Lib.) de Bary is the fungal agent that causes stem rot disease in oilseed rape ( Brassica spp.). To overcome plant cell wall during early pathogenesis, the fungus secretes several types of cell wall-degrading enzymes such as polygalacturonases (PGs). The activities of these enzymes determine the pathogenicity/ virulence and are crucial for the colonization on plant tissues. PGs can induce defense reactions in plants unrelated to its enzyme activities. To understand the PG signaling pathway, a PG gene was cloned from S. sclerotiorum by RT-PCR. The encoding region of the PG gene was fused to the yeast GAL4 DNA-binding domain in yeast expression vector PGBKT7 and a rapeseed ( B. napus) cDNA expression library was constructed in yeast. PG-interacting proteins were screened in the library using PG as bait by yeast two-hybrid assay. An interacting protein was isolated. Sequencing and BLAST analysis revealed that the protein contained a C2-domain and was predicted to be a Ca 2+ binding domain. The protein shared 80.24% identity in amino acids with a C2-domain protein in Arabidopsis with unknown function. The expression levels of the C2-domain protein in floral, leaf, and stem organs of oilseed rape were investigated by semi-quantitative RT-PCR. The C2-domain protein was highly expressed in leaves when inoculated with S. sclerotiorum. The comparisons of the C2-domain proteins identified in oilseed rape with that of other species suggested that aspartic acid residues involving in Ca 2+ binding were conserved.