Identification of a S-ribonuclease-binding protein in Petunia hybrida

Identification of a S-ribonuclease-binding protein in Petunia hybrida To investigate protein-protein interactions in gametophytic self-incompatibility, we used a yeast two-hybrid assay to identify proteins that could interact with the S-ribonuclease protein. These assays identified a pollen-expressed protein, which we have named PhSBP1, that appears to bind with a high degree of specificity to the Petunia hybrida S-ribonuclease. Although PhSBP1 activates reporter gene expression only when expressed in tandem with a S-RNAse bait protein, binding is not allele-specific. Sequence analysis demonstrated that PhSBP1 contained a C-terminal cysteine-rich region that includes a RING-HC domain. Because many RING-finger domain proteins appear to function as E3 ubiquitin ligases, our results suggest that ubiquitination and protein degradation may play a role in regulating self-incompatibility interactions. Together, these results suggest that PhSBP1 may be a candidate for the recently proposed general inhibitor (RI) of self-incompatibility ribonucleases. Plant Molecular Biology Springer Journals

Identification of a S-ribonuclease-binding protein in Petunia hybrida

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Kluwer Academic Publishers
Copyright © 2001 by Kluwer Academic Publishers
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
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