SCF(SLF)-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida.
Front Genet. 2014; 5:228.FG

Abstract

Many flowering plants adopt self-incompatibility (SI) to maintain their genetic diversity. In species of Solanaceae, Plantaginaceae, and Rosaceae, SI is genetically controlled by a single S-locus with multiple haplotypes. The S-locus has been shown to encode S-RNases expressed in pistil and multiple SLF (S-locus F-box) proteins in pollen controlling the female and male specificity of SI, respectively. S-RNases appear to function as a cytotoxin to reject self-pollen. In addition, SLFs have been shown to form SCF (SKP1/Cullin1/F-box) complexes to serve as putative E3 ubiquitin ligase to interact with S-RNases. Previously, two different mechanisms, the S-RNase degradation and the S-RNase compartmentalization, have been proposed as the restriction mechanisms of S-RNase cytotoxicity allowing compatible pollination. In this study, we have provided several lines of evidence in support of the S-RNase degradation mechanism by a combination of cellular, biochemical and molecular biology approaches. First, both immunogold labeling and subcellular fractionation assays showed that two key pollen SI factors, PhS3L-SLF1 and PhSSK1 (SLF-interacting SKP1-like1) from Petunia hybrida, a Solanaceous species, are co-localized in cytosols of both pollen grains and tubes. Second, PhS3L-RNases are mainly detected in the cytosols of both self and non-self-pollen tubes after pollination. Third, we found that PhS-RNases selectively interact with PhSLFs by yeast two-hybrid and co-immunoprecipitation assays. Fourth, S-RNases are specifically degraded in compatible pollen tubes by non-self SLF action. Taken together, our results demonstrate that SCF(SLF-mediated) non-self S-RNase degradation occurs in the cytosol of pollen tube through the ubiquitin/26S proteasome system serving as the major mechanism to neutralize S-RNase cytotoxicity during compatible pollination in P. hybrida.

Links

PMC Free PDF

Authors+Show Affiliations

Liu W

State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research Beijing, China ; University of Chinese Academy of Sciences Beijing, China.

State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research Beijing, China.

Zhang Y

State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research Beijing, China.

Xue Y

State Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences and National Center for Plant Gene Research Beijing, China.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

25101113

Citation

Liu, Wei, et al. "SCF(SLF)-mediated Cytosolic Degradation of S-RNase Is Required for Cross-pollen Compatibility in S-RNase-based Self-incompatibility in Petunia Hybrida." Frontiers in Genetics, vol. 5, 2014, p. 228.

Liu W, Fan J, Li J, et al. SCF(SLF)-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida. Front Genet. 2014;5:228.

Liu, W., Fan, J., Li, J., Song, Y., Li, Q., Zhang, Y., & Xue, Y. (2014). SCF(SLF)-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida. Frontiers in Genetics, 5, 228. https://doi.org/10.3389/fgene.2014.00228

Liu W, et al. SCF(SLF)-mediated Cytosolic Degradation of S-RNase Is Required for Cross-pollen Compatibility in S-RNase-based Self-incompatibility in Petunia Hybrida. Front Genet. 2014;5:228. PubMed PMID: 25101113.

* Article titles in AMA citation format should be in sentence-case

TY - JOUR T1 - SCF(SLF)-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida. AU - Liu,Wei, AU - Fan,Jiangbo, AU - Li,Junhui, AU - Song,Yanzhai, AU - Li,Qun, AU - Zhang,Yu'e, AU - Xue,Yongbiao, Y1 - 2014/07/22/ PY - 2013/12/26/received PY - 2014/06/30/accepted PY - 2014/8/8/entrez PY - 2014/8/8/pubmed PY - 2014/8/8/medline KW - S-RNase localization KW - SCFSLF KW - cross-pollen compatibility KW - self-incompatibility KW - self-pollen incompatibility KW - ubiquitin/26S proteasome system SP - 228 EP - 228 JF - Frontiers in genetics JO - Front Genet VL - 5 N2 - Many flowering plants adopt self-incompatibility (SI) to maintain their genetic diversity. In species of Solanaceae, Plantaginaceae, and Rosaceae, SI is genetically controlled by a single S-locus with multiple haplotypes. The S-locus has been shown to encode S-RNases expressed in pistil and multiple SLF (S-locus F-box) proteins in pollen controlling the female and male specificity of SI, respectively. S-RNases appear to function as a cytotoxin to reject self-pollen. In addition, SLFs have been shown to form SCF (SKP1/Cullin1/F-box) complexes to serve as putative E3 ubiquitin ligase to interact with S-RNases. Previously, two different mechanisms, the S-RNase degradation and the S-RNase compartmentalization, have been proposed as the restriction mechanisms of S-RNase cytotoxicity allowing compatible pollination. In this study, we have provided several lines of evidence in support of the S-RNase degradation mechanism by a combination of cellular, biochemical and molecular biology approaches. First, both immunogold labeling and subcellular fractionation assays showed that two key pollen SI factors, PhS3L-SLF1 and PhSSK1 (SLF-interacting SKP1-like1) from Petunia hybrida, a Solanaceous species, are co-localized in cytosols of both pollen grains and tubes. Second, PhS3L-RNases are mainly detected in the cytosols of both self and non-self-pollen tubes after pollination. Third, we found that PhS-RNases selectively interact with PhSLFs by yeast two-hybrid and co-immunoprecipitation assays. Fourth, S-RNases are specifically degraded in compatible pollen tubes by non-self SLF action. Taken together, our results demonstrate that SCF(SLF-mediated) non-self S-RNase degradation occurs in the cytosol of pollen tube through the ubiquitin/26S proteasome system serving as the major mechanism to neutralize S-RNase cytotoxicity during compatible pollination in P. hybrida. SN - 1664-8021 UR - https://www.unboundmedicine.com/medline/citation/25101113/SCF_SLF__mediated_cytosolic_degradation_of_S_RNase_is_required_for_cross_pollen_compatibility_in_S_RNase_based_self_incompatibility_in_Petunia_hybrida_ DB - PRIME DP - Unbound Medicine ER -

Tags

SCF(SLF)-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida.Front Genet. 2014; 5:228.FG

Links

Authors+Show Affiliations

Pub Type(s)

Language

PubMed ID

Citation

SCF(SLF)-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida.
Front Genet. 2014; 5:228.FG