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

Penglin Sun, Shu Li, Dihong Lu, Justin S. Williams, Teh-hui Kao

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

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-RNase, 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-RNase(s), with which the SLF interacts, via the ubiquitin-26S proteasome pathway. A complete set of SLFs is required to detoxify all non-self S-RNases to allow cross-compatible pollination. Here, we show that SLF1 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 S2-SLF1 (SLF1 of S2 haplotype) that contains a degradation motif. Seven of the 18 amino acids are conserved among all 17 SLF proteins of S2 haplotype and S3 haplotype involved in pollen specificity, suggesting that all SLF proteins are probably subject to similar degradation. Deleting the 18 amino acid sequence from S2-SLF1 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. Significance Statement S-locus F-box (SLF) proteins mediate degradation of all non-self S-RNases via the ubiquitin-26S proteasome pathway (UPP), and in this work, we report that SLF proteins themselves are subject to degradation via UPP and that deleting the sequence containing a degron, though stabilizing the proteins, abolishes their function in self-incompatibility.

Original languageEnglish (US)
Pages (from-to)213-223
Number of pages11
JournalPlant Journal
Volume83
Issue number2
DOIs
StatePublished - Jan 1 2015

All Science Journal Classification (ASJC) codes

  • Genetics
  • Plant Science
  • Cell Biology

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