Abstract
A defective S-allele, S0, and a functional S-allele, Sx, have previously been found to be retained in an F1 hybrid of a self-compatible commercial cultivar of Petunia hybrida. Pistil proteins associated with these two alleles have also been identified. Their amino-terminal sequences have been found to share a high degree of similarity with those of S-proteins characterized from self-incompatible solanaceous species. Here we report the isolation and sequencing of cDNAs encoding S0- and Sx-proteins. Their deduced amino acid sequences contain all the consensus primary structural features of S-proteins from self-incompatible solanaceous species. Both proteins also have ribonuclease activity. The implications of these findings are discussed in relation to the presumed function of the S-protein in the self-incompatibility interaction.
Original language | English (US) |
---|---|
Pages (from-to) | 523-528 |
Number of pages | 6 |
Journal | Plant molecular biology |
Volume | 19 |
Issue number | 3 |
DOIs | |
State | Published - Jun 1992 |
All Science Journal Classification (ASJC) codes
- Agronomy and Crop Science
- Genetics
- Plant Science