%A Liu,Wei
%A Fan,Jiangbo
%A Li,Junhui
%A Song,Yanzhai
%A Li,Qun
%A Zhang,Yu'e
%A Xue,Yongbiao
%D 2014
%J Frontiers in Genetics
%C
%F
%G English
%K self-incompatibility,self-pollen incompatibility,cross-pollen compatibility,S-RNase localization,SCFSLF,ubiquitin/26S proteasome system
%Q
%R 10.3389/fgene.2014.00228
%W
%L
%M
%P
%7
%8 2014-July-22
%9 Original Research
%+ Dr Yongbiao Xue,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,ybxue@genetics.ac.cn
%#
%! SCFSLF-mediated cytosolic degradation of S-RNase
%*
%<
%T SCFSLF-mediated cytosolic degradation of S-RNase is required for cross-pollen compatibility in S-RNase-based self-incompatibility in Petunia hybrida
%U https://www.frontiersin.org/articles/10.3389/fgene.2014.00228
%V 5
%0 JOURNAL ARTICLE
%@ 1664-8021
%X 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 SCFSLF-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.