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Journal of Experimental Botany, Vol. 54, No. 380, pp. 149-156, January 1, 2003
© 2003 Oxford University Press

Molecular mechanism of self-recognition in Brassica self-incompatibility

Received 22 May 2002; Accepted 7 August 2002

Seiji Takayama1, and Akira Isogai

Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0101, Japan

1 To whom correspondence should be addressed. Fax: +81 743 72 5459. E-mail: takayama{at}bs.aist-nara.ac.jp

In most self-incompatible plant species, recognition of self-pollen is controlled by a single locus, termed the S-locus. In Brassica, genetic dissection of the S-locus has revealed the presence of three highly-polymorphic genes: S-receptor kinase (SRK), S-locus protein 11 (SP11) (also known as 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 stigma. SP11 encodes a small cysteine-rich protein that determines the S-haplotype specificity of pollen. SLG encodes a secreted form of stigma protein similar to the extracellular domain of SRK. Recent biochemical studies have revealed that SP11 functions as the sole ligand for its cognate SRK receptor complex. Their interaction induces the autophosphorylation of SRK, which is expected to trigger the signalling cascade that results in the rejection of self-pollen. This so-called ligand–receptor complex interaction and receptor activation occur in an S-haplotype-specific manner, and this specificity is almost certainly the basis for self-pollen recognition.

Key words: Brassica, ligand, receptor, self-incompatibility, SLG, SP11, SRK.


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