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


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.

SUBMITTER: Chookajorn T 

PROVIDER: S-EPMC327116 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature

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

Chookajorn Thanat T   Kachroo Aardra A   Ripoll Daniel R DR   Clark Andrew G AG   Nasrallah June B JB  

Proceedings of the National Academy of Sciences of the United States of America 20031223 4


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 i  ...[more]

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