The amino terminal F-box domain of Petunia inflata S-locus F-box protein is involved in the S-RNase-based self-incompatibility mechanism

Xiaoying Meng, Zhihua Hua, Penglin Sun, Teh-hui Kao

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Background and aims: Pistils 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 results: To examine whether the F-box domain of PiSLF is required for SI function, we expressed a truncated PiSLF2 (S2 allelic variant) without this domain in S2S3 plants and showed that, unlike the full-length PiSLF2, it did not cause breakdown of SI in S3 pollen. We identified PiSSK1 (P. inflata SSK1) and found that it did not interact with PiSLF1, PiSLF2 or PiSLF3. Conclusions: The finding that the truncated PiSLF2 did not cause breakdown of SI in S3 transgenic pollen suggests that the F-box domain of PiSLF2 is required for mediating degradation of S3-RNase, a non-self S-RNase, in S3 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.

Original languageEnglish (US)
Article numberplr016
JournalAoB PLANTS
Volume11
Issue number1
DOIs
StatePublished - Dec 1 2011

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Petunia integrifolia
F-box proteins
loci
pollen
pistil
Antirrhinum hispanicum
Petunia hybrida
degradation
proteasome endopeptidase complex
Angiospermae
genes
Arabidopsis thaliana
proteins
genetically modified organisms

All Science Journal Classification (ASJC) codes

  • Plant Science

Cite this

@article{15fca61a35eb494a834f666a1e31f76f,
title = "The amino terminal F-box domain of Petunia inflata S-locus F-box protein is involved in the S-RNase-based self-incompatibility mechanism",
abstract = "Background and aims: Pistils 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 results: To examine whether the F-box domain of PiSLF is required for SI function, we expressed a truncated PiSLF2 (S2 allelic variant) without this domain in S2S3 plants and showed that, unlike the full-length PiSLF2, it did not cause breakdown of SI in S3 pollen. We identified PiSSK1 (P. inflata SSK1) and found that it did not interact with PiSLF1, PiSLF2 or PiSLF3. Conclusions: The finding that the truncated PiSLF2 did not cause breakdown of SI in S3 transgenic pollen suggests that the F-box domain of PiSLF2 is required for mediating degradation of S3-RNase, a non-self S-RNase, in S3 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.",
author = "Xiaoying Meng and Zhihua Hua and Penglin Sun and Teh-hui Kao",
year = "2011",
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doi = "10.1093/aobpla/plr016",
language = "English (US)",
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journal = "AoB PLANTS",
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The amino terminal F-box domain of Petunia inflata S-locus F-box protein is involved in the S-RNase-based self-incompatibility mechanism. / Meng, Xiaoying; Hua, Zhihua; Sun, Penglin; Kao, Teh-hui.

In: AoB PLANTS, Vol. 11, No. 1, plr016, 01.12.2011.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The amino terminal F-box domain of Petunia inflata S-locus F-box protein is involved in the S-RNase-based self-incompatibility mechanism

AU - Meng, Xiaoying

AU - Hua, Zhihua

AU - Sun, Penglin

AU - Kao, Teh-hui

PY - 2011/12/1

Y1 - 2011/12/1

N2 - Background and aims: Pistils 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 results: To examine whether the F-box domain of PiSLF is required for SI function, we expressed a truncated PiSLF2 (S2 allelic variant) without this domain in S2S3 plants and showed that, unlike the full-length PiSLF2, it did not cause breakdown of SI in S3 pollen. We identified PiSSK1 (P. inflata SSK1) and found that it did not interact with PiSLF1, PiSLF2 or PiSLF3. Conclusions: The finding that the truncated PiSLF2 did not cause breakdown of SI in S3 transgenic pollen suggests that the F-box domain of PiSLF2 is required for mediating degradation of S3-RNase, a non-self S-RNase, in S3 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.

AB - Background and aims: Pistils 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 results: To examine whether the F-box domain of PiSLF is required for SI function, we expressed a truncated PiSLF2 (S2 allelic variant) without this domain in S2S3 plants and showed that, unlike the full-length PiSLF2, it did not cause breakdown of SI in S3 pollen. We identified PiSSK1 (P. inflata SSK1) and found that it did not interact with PiSLF1, PiSLF2 or PiSLF3. Conclusions: The finding that the truncated PiSLF2 did not cause breakdown of SI in S3 transgenic pollen suggests that the F-box domain of PiSLF2 is required for mediating degradation of S3-RNase, a non-self S-RNase, in S3 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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