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Molecular Plant Advance Access published online on June 26, 2008

Molecular Plant, doi:10.1093/mp/ssn032
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© The Author 2008. Published by the Molecular Plant Shanghai Editorial Office in association with Oxford University Press on behalf of CSPP and IPPE, SIBS, CAS.

Biochemical Models for S-RNase-Based Self-Incompatibility

Zhi-Hua Huaa,c, Allison Fieldsb and Teh-hui Kaoa,b,1

a Intercollege Graduate Degree Program in Plant Biology, The Pennsylvania State University, University Park, PA 16802, USA
b Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA
c Present address: Department of Genetics, University of Wisconsin, Madison, WI 53706, USA

1 To whom correspondence should be addressed. E-mail txk3{at}psu.edu, fax (814) 863-7024, tel. (814) 863-1042.

S-RNase-based self-incompatibility (SI) is a genetically determined self/non-self-recognition process employed by many flowering plant species to prevent inbreeding and promote outcrosses. For the Plantaginaceae, Rosaceae and Solanaceae, it is now known that S-RNase and S-locus F-box (two multiple allelic genes at the S-locus) determine the female and male specificity, respectively, during SI interactions. However, how allelic products of these two genes interact inside pollen tubes to result in specific growth inhibition of self-pollen tubes remains to be investigated. Here, we review all the previously proposed biochemical models and discuss whether their predictions are consistent with all SI phenomena, including competitive interaction where SI breaks down in pollen that carries two different pollen S-alleles. We also discuss these models in light of the recent findings of compartmentalization of S-RNases in both incompatible and compatible pollen tubes. Lastly, we summarize the results from our recent biochemical studies of PiSLF (Petunia inflata SLF) and S-RNase, and present a new model for the biochemical mechanism of SI in the Solanaceae. The tenet of this model is that a PiSLF preferentially interacts with its non-self S-RNases in the cytoplasm of a pollen tube to result in the assembly of an E3-like complex, which then mediates ubiquitination and degradation of non-self S-RNases through the ubiquitin–26S proteasome pathway. This model can explain all SI phenomena and, at the same time, has raised new questions for further study.


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