Direct ligand-receptor complex interaction controls Brassica self-incompatibility

Seiji Takayama, Hiroko Shimosato, Hiroshi Shiba, Miyuki Funato, Fang Sik Che, Masao Watanabe, Megumi Iwano, Akira Isogai

Research output: Contribution to journalArticlepeer-review

319 Citations (Scopus)

Abstract

Many higher plants have evolved self-incompatibility mechanisms to prevent self-fertilization. In Brassica self-incompatibility, recognition between pollen and the stigma is controlled by the S locus, which contains three highly polymorphic genes: S-receptor kinase (SRK), S-locus protein 11 (SP11) (also called S-locus cysteine-rich protein; SCR) and S-locus glycoprotein (SLG). SRK encodes a membrane-spanning serine/threonine kinase that determines the S-haplotype specificity of the stigma6, and SP11 encodes a small cysteine-rich protein that determines the S-haplotype specificity of pollen. SP11 is localized in the pollen coat. It is thought that, during self-pollination, SP11 is secreted from the pollen coat and interacts with its cognate SRK in the papilla cell of the stigma to elicit the self-incompatibility response. SLG is a secreted stigma protein that is highly homologous to the SRK extracellular domain. Although it is not required for S-haplotype specificity of the stigma, SLG enhances the self-incompatibility response; however, how this is accomplished remains controversial. Here we show that a single form of SP11 of the S8 haplotype (S8-SP11) stabilized with four intramolecular disulphide bonds specifically binds the stigma membrane of the S8 haplotype to induce autophosphorylation of SRK8, and that SRK8 and SLG8 together form a high-affinity receptor complex for S8-SP11 on the stigma membrane.

Original languageEnglish
Pages (from-to)534-538
Number of pages5
JournalNature
Volume413
Issue number6855
DOIs
Publication statusPublished - 2001 Oct 4
Externally publishedYes

ASJC Scopus subject areas

  • General

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