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

doi:10.1111/j.1469-8137.2007.02126.x

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Wiley InterScience

New Phytologist

Volume 175 Issue 4, Pages 619 - 629

Published Online: 11 Jun 2007

Published on behalf of the New Phytologist Trust

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

Benjamin P. Kemp and James Doughty

Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK

Author for correspondence: James Doughty Tel: +44 1225383485 Fax: +44 1225826779 Email: bssjd@bath.ac.uk

KEYWORDS

peptide mapping • receptor • recognition • S cysteine-rich • S-locus receptor kinase • self-incompatibility

New Phytologist (2007) 175: 619–629

doi: 10.1111/j.1469-8137.2007.02126.x

ABSTRACT

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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.
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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.
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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.
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We show that residues within the hypervariable subdomain define SRK binding and are likely to be involved in defining haplotype specificity.