期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 4, 页码 911-917出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2637116100
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资金
- NIGMS NIH HHS [GM57527, R01 GM057527] Funding Source: Medline
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.
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