Specificity determinants and diversification of the Brassica self-incompatibility pollen ligand

Proc Natl Acad Sci U S A. 2004 Jan 27;101(4):911-7. doi: 10.1073/pnas.2637116100. Epub 2003 Dec 23.

Abstract

Self-incompatibility in crucifers is effected by allele-specific interactions between the highly polymorphic stigmatic S locus receptor kinase (SRK) and its pollen ligand, the S locus cysteine-rich protein (SCR). Here we show that specificity in SCR function is determined by four contiguous amino acids in one variant, indicating that the minimum sequence requirement for gaining a new specificity can be low. We also provide evidence for an extraordinarily high degree of evolutionary flexibility in SCR, whereby SCR can tolerate extensive amino acid changes within the limits of maintaining the same predicted overall structure. This remarkable adaptability suggests a hypothesis for generation of new self-incompatibility specificities by gradual modification of SRK-SCR affinities and, more generally, for functional specialization within families of homologous ligands and receptors.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Brassica / enzymology
  • Brassica / genetics
  • Brassica / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Mutagenesis
  • Plant Proteins
  • Pollen / metabolism*
  • Protein Conformation
  • Protein Kinases / chemistry
  • Protein Kinases / genetics*
  • Sequence Homology, Amino Acid

Substances

  • Plant Proteins
  • Protein Kinases
  • S-receptor kinase