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
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