The Skp1-like protein SSK1 is required for cross-pollen compatibility in S-RNase-based self-incompatibility

74Citations
Citations of this article
45Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

The self-incompatibility (SI) response occurs widely in flowering plants as a means of preventing self-fertilization. In these selfnon-self discrimination systems, plant pistils reject self or genetically related pollen. In the Solanaceae, Plantaginaceae and Rosaceae, pistil-secreted S-RNases enter the pollen tube and function as cytotoxins to specifically arrest self-pollen tube growth. Recent studies have revealed that the S-locus F-box (SLF) protein controls the pollen expression of SI in these families. However, the precise role of SLF remains largely unknown. Here we report that PhSSK1 (Petunia hybrida SLF-interacting Skp1-like1), an equivalent of AhSSK1 of Antirrhinum hispanicum, is expressed specifically in pollen and acts as an adaptor in an SCF(Skp1-Cullin1-F-box)SLF complex, indicating that this pollen-specific SSK1-SLF interaction occurs in both Petunia and Antirrhinum, two species from the Solanaceae and Plantaginaceae, respectively. Substantial reduction of PhSSK1 in pollen reduced cross-pollen compatibility (CPC) in the S-RNase-based SI response, suggesting that the pollen S determinant contributes to inhibiting rather than protecting the S-RNase activity, at least in solanaceous plants. Furthermore, our results provide an example that a specific Skp1-like protein other than the known conserved ones can be recruited into a canonical SCF complex as an adaptor. © 2010 Blackwell Publishing Ltd.

Cite

CITATION STYLE

APA

Zhao, L., Huang, J., Zhao, Z., Li, Q., Sims, T. L., & Xue, Y. (2010). The Skp1-like protein SSK1 is required for cross-pollen compatibility in S-RNase-based self-incompatibility. Plant Journal, 62(1), 52–63. https://doi.org/10.1111/j.1365-313X.2010.04123.x

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free