The zinc finger C(36)-X1-C(38)-X7-C(46)-X6-H(53) of the nuclearly localized C2 protein of Tomato yellow leaf curl virus China is involved in pathogenicity and suppression of posttranscriptional gene silencing (PTGS). Here, we demonstrate that the zinc finger is indispensable for the C2 protein to bind zinc and DNA. Mutation of cysteine residue C(36), C(38), or C(46) reduced the zinc and DNA binding capacity of C2 protein. When expressed from potato virus X, all three mutants, C2-C(36)R, C2-C(38)N, and C2-C(46)I, tagged with a green fluorescent protein (GFP) were still capable of transporting GFP into but aggregated abnormally in nuclei. Our data establish that zinc- and DNA-binding activity correlates with C2-mediated pathogenesis and PTGS suppression.