S cysteine-rich (SCR) binding domain analysis of the Brassica self-incompatibility S-locus receptor kinase

Brassica self-incompatibility, a highly discriminating outbreeding mechanism, has become a paradigm for the study of plant cell-cell communications. When self-pollen lands on a stigma, the male ligand S cysteine-rich (SCR), which is present in the pollen coat, is transmitted to the female receptor,...

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Veröffentlicht in:The New phytologist. - 1979. - 175(2007), 4 vom: 23., Seite 619-629
1. Verfasser: Kemp, Benjamin P (VerfasserIn)
Weitere Verfasser: Doughty, James
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2007
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Plant Proteins Recombinant Proteins
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245 1 2 |a S cysteine-rich (SCR) binding domain analysis of the Brassica self-incompatibility S-locus receptor kinase 
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500 |a CommentIn: New Phytol. 2007;175(4):597-9. - PMID 17688575 
500 |a Citation Status MEDLINE 
520 |a Brassica self-incompatibility, a highly discriminating outbreeding mechanism, has become a paradigm for the study of plant cell-cell communications. When self-pollen lands on a stigma, the male ligand S cysteine-rich (SCR), which is present in the pollen coat, is transmitted to the female receptor, S-locus receptor kinase (SRK). SRK is a membrane-spanning serine/threonine receptor kinase present in the stigmatic papillar cell membrane. Haplotype-specific binding of SCR to SRK brings about pollen rejection. The extracellular receptor domain of SRK (eSRK) is responsible for binding SCR. Based on sequence homology, eSRK can be divided into three subdomains: B lectin-like, hypervariable, and PAN. Biochemical analysis of these subdomains showed that the hypervariable subdomain is responsible for most of the SCR binding capacity of eSRK, whereas the B lectin-like and PAN domains have little, if any, affinity for SCR. Fine mapping of the SCR binding region of SRK using a peptide array revealed a region of the hypervariable subdomain that plays a key role in binding the SCR molecule. We show that residues within the hypervariable subdomain define SRK binding and are likely to be involved in defining haplotype specificity 
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