Pollen S–locus F–box proteins of Petunia involved in S–RNase‐based self‐incompatibility are themselves subject to ubiquitin‐mediated degradation

Summary Many flowering plants show self‐incompatibility, an intra‐specific reproductive barrier by which pistils reject self‐pollen to prevent inbreeding and accept non‐self pollen to promote out‐crossing. In Petunia , the polymorphic S–locus determines self/non‐self recognition. The locus contains a gene encoding an S– RN ase, which controls pistil specificity, and multiple S‐locus F‐box ( SLF ) genes that collectively control pollen specificity. Each SLF is a component of an SCF (Skp1/Cullin/F‐box) complex that is responsible for mediating degradation of non‐self S‐ RN ase(s), with which the SLF interacts, via the ubiquitin–26S proteasome pathway. A complete set of SLF s is required to detoxify all non‐self S‐ RN ases to allow cross‐compatible pollination. Here, we show that SLF 1 of Petunia inflata is itself subject to degradation via the ubiquitin–26S proteasome pathway, and identify an 18 amino acid sequence in the C‐terminal region of S 2 ‐ SLF 1 ( SLF 1 of S 2 haplotype) that contains a degradation motif. Seven of the 18 amino acids are conserved among all 17 SLF proteins of S 2 haplotype and S 3 haplotype involved in pollen specificity, suggesting that all SLF proteins are probably subject to similar degradation. Deleting the 18 amino acid sequence from S 2 ‐ SLF 1 stabilized the protein but abolished its function in self‐incompatibility, suggesting that dynamic cycling of SLF proteins is an integral part of their function in self‐incompatibility.