Journal of Experimental Botany, Vol. 54, No. 380, pp. 123-130,
January 1, 2003
© 2003 Oxford University Press
S-RNase complexes and pollen rejection
Received 22 May 2002; Accepted 24 September 2002
1 Department of Biochemistry, Facultad de Química, National Autonomous University of México, Conjunto E Paseo de la Investigacion Cientifica, Ciudad Universitaria, 04510 México D.F., México
2 Department of Biochemistry, University of Missouri-Columbia, 117 Schweitzer Hall, Columbia, MO 65211, USA
3 To whom correspondence should be addressed. Fax: +1 573 882 5635. E-mail: mcclureb{at}missouri.edu
Biochemical interactions between the pollen and the pistil allow plants fine control over fertilization. S-RNase-based pollen rejection is among the most widespread and best understood of these interactions. At least three plant families have S-RNase-based self-incompatibility (SI) systems, and S-RNases have also been implicated in interspecific pollen rejection. Although S-RNases determine the specificity of SI, other genes are required for the pollen rejection system to function. Progress is being made toward identifying these non-S-RNase factors. HT-protein, first identified as a non-S-RNase factor that was required for SI in Nicotiana alata, has now been implicated in other species as well. In addition, several pistil proteins bind to S-RNase in vitro. One hypothesis is that S-RNase forms a complex with these proteins in vivo that is the active form of S-RNase in pollen rejection.
Key words: Interspecific incompatibility, pollenpistil interactions, self-incompatibility, S-locus, S-RNase.
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