ArticleAoB PLANTS2011
The amino terminal F-box domain of Petunia inflata S-locus F-box protein is involved in the S-RNase-based self-incompatibility mechanism.
Article in AoB PLANTS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Analyses of Cullin1 homologs reveal functional redundancy in S-RNase-based self-incompatibility and evolutionary relationships in eudicots.The Plant cell · 2023Article
- Caspase-like proteases and the phytohormone cytokinin as determinants of S-RNAse-based self-incompatibility-induced PCD in Petunia hybrida L.Protoplasma · 2021Article
- S-Locus F-Box Proteins Are Solely Responsible for S-RNase-Based Self-Incompatibility ofThe Plant cell · 2018Article
- CRISPR/Cas9-mediated knockout of PiSSK1 reveals essential role of S-locus F-box protein-containing SCF complexes in recognition of non-self S-RNases during cross-compatible pollination in self-incompatible Petunia inflata.Plant reproduction · 2018Article
- Insight into S-RNase-based self-incompatibility in Petunia: recent findings and future directions.Frontiers in plant science · 2015Article
- Identification of the self-incompatibility locus F-box protein-containing complex in Petunia inflata.Plant reproduction · 2014Article
- Identification of SFBB-containing canonical and noncanonical SCF complexes in pollen of apple (Malus × domestica).PloS one · 2014Article
- A new dual-specific incompatibility allele revealed by absence of glycosylation in the conserved C2 site of a Solanum chacoense S-RNase.Journal of experimental botany · 2013Article
- Self-incompatibility in Petunia inflata: the relationship between a self-incompatibility locus F-box protein and its non-self S-RNases.The Plant cell · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BACKGROUND AND
aimsPistils of flowering plants possessing self-incompatibility (SI) can distinguish between self and non-self pollen, and only allow non-self pollen to effect fertilization. For Petunia inflata, the S-RNase gene encodes pistil specificity and multiple S-locus F-box (SLF) genes encode pollen specificity. Each SLF produced in pollen interacts with a subset of non-self S-RNases to mediate their ubiquitination and degradation by the 26S proteasome. RATIONALE: S-locus F-box has been proposed to function as a component of the conventional SCF (SKP1-CULLIN-F-box protein) complex, based on the finding that two SKP1-like proteins, AhSSK1 (Antirrhinum hispanicum SLF-interacting SKP1-like1) and PhSSK1 (Petunia hybrida SSK1), interact with the F-box domain of some allelic variants of SLF. However, we previously showed that PiSLF (P. inflata SLF) did not interact with any SKP1 of P. inflata or Arabidopsis thaliana, but instead interacted with a RING-finger protein, PiSBP1 (P. inflata S-RNase-Binding Protein1), which may also play the role of SKP1. Thus, the biochemical nature of the SLF-containing complex is as yet unclear. PRINCIPAL
resultsTo examine whether the F-box domain of PiSLF is required for SI function, we expressed a truncated PiSLF(2) (S(2) allelic variant) without this domain in S(2)S(3) plants and showed that, unlike the full-length PiSLF(2), it did not cause breakdown of SI in S(3) pollen. We identified PiSSK1 (P. inflata SSK1) and found that it did not interact with PiSLF(1), PiSLF(2) or PiSLF(3).
conclusionsThe finding that the truncated PiSLF(2) did not cause breakdown of SI in S(3) transgenic pollen suggests that the F-box domain of PiSLF(2) is required for mediating degradation of S(3)-RNase, a non-self S-RNase, in S(3) pollen, and thus is required for SI function. The finding that PiSSK1 did not interact with three allelic variants of PiSLF is consistent with our previous finding that PiSLF might not be in a conventional SCF complex.
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