Self-compatibility in aLycopersicon peruvianum variant (LA2157) is associated with a lack of style S-RNase activity.

A series of crosses between a naturally-occurring self-compatible accession ofLycopersicon peruvianum and a closely-related self-incompatible accession were used to demonstrate that the mutation to self-compatibility is located at the S-locus. Progeny of the crosses contain abundant style proteins of about 30 kDa that segregate with the S6and S7-alleles from the SI parent and the Sc-allele from the SC parent. The S6and S7-associated proteins have ribonuclease activity whereas the Sc-associated protein is not an active ribonuclease. This finding indicates that S-RNases are determinants of self-incompatibility in the style and that the ribonuclease activity is essential for their function.