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Ubiquitination of S-4-RNase by S-LOCUS F-BOX LIKE2 Contributes to Self-Compatibility of Sweet Cherry 'Lapins'

文献类型： 外文期刊

作者： Li, Yang 1 ; Duan, Xuwei 2 ; Wu, Chuanbao 1 ; Yu, Jie 1 ; Liu, Chunsheng 1 ; Wang, Jing 2 ; Zhang, Xiaoming 2 ; Yan, Guoh 1 ;

作者机构： 1.China Agr Univ, Lab Fruit Cell & Mol Breeding, Beijing 100193, Peoples R China

2.Beijing Acad Agr & Forestry Sci, Inst Forestry & Pomol, Beijing 100097, Peoples R China

期刊名称：PLANT PHYSIOLOGY （ 影响因子：8.34； 五年影响因子：8.972 ）

ISSN： 0032-0889

年卷期： 2020 年 184 卷 4 期

页码：

收录情况： SCI

摘要： An F-box protein contributes to the self-compatibility of sweet cherry 'Lapins'. Recent studies have shown that loss of pollen-S function in S-4 ' pollen from sweet cherry (Prunus avium) is associated with a mutation in an S haplotype-specific F-box4 (SFB4) gene. However, how this mutation leads to self-compatibility is unclear. Here, we examined this mechanism by analyzing several self-compatible sweet cherry varieties. We determined that mutated SFB4 (SFB4') in S4 ' pollen (pollen harboring the SFB4' gene) is approximately 6 kD shorter than wild-type SFB4 due to a premature termination caused by a four-nucleotide deletion. SFB4 ' did not interact with S-RNase. However, a protein in S4 ' pollen ubiquitinated S-RNase, resulting in its degradation via the 26S proteasome pathway, indicating that factors in S4 ' pollen other than SFB4 participate in S-RNase recognition and degradation. To identify these factors, we used S-4-RNase as a bait to screen S4 ' pollen proteins. Our screen identified the protein encoded by S-4-SLFL2, a low-polymorphic gene that is closely linked to the S-locus. Further investigations indicate that SLFL2 ubiquitinates S-RNase, leading to its degradation. Subcellular localization analysis showed that SFB4 is primarily localized to the pollen tube tip, whereas SLFL2 is not. When S-4-SLFL2 expression was suppressed by antisense oligonucleotide treatment in wild-type pollen tubes, pollen still had the capacity to ubiquitinate S-RNase; however, this ubiquitin-labeled S-RNase was not degraded via the 26S proteasome pathway, suggesting that SFB4 does not participate in the degradation of S-RNase. When SFB4 loses its function, S-4-SLFL2 might mediate the ubiquitination and degradation of S-RNase, which is consistent with the self-compatibility of S4 ' pollen.

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