Present address: Departamento de Bioquimica, Facultad de Quimica, Universidad Nacional Autonoma de Mexico, Ave Universidad y Copilco, Mexico D.F. 04510, Mexico.
Stylar glycoproteins bind to S-RNase in vitro
Article first published online: 28 FEB 2005
The Plant Journal
Volume 42, Issue 3, pages 295–304, May 2005
How to Cite
Cruz-Garcia, F., Nathan Hancock, C., Kim, D. and McClure, B. (2005), Stylar glycoproteins bind to S-RNase in vitro. The Plant Journal, 42: 295–304. doi: 10.1111/j.1365-313X.2005.02375.x
- Issue published online: 28 FEB 2005
- Article first published online: 28 FEB 2005
- Received 16 November 2004; revised 30 December 2004; accepted 7 January 2005.
S-RNases determine the specificity of S-specific pollen rejection in self-incompatible plants of the Solanaceae, Rosaceae, and Scrophulariaceae. They are also implicated in at least two distinct types of unilateral interspecific incompatibility in Nicotiana. However, S-RNase itself is not sufficient for most types of pollen rejection, and evidence for its direct interaction with pollen tubes is limited. Thus, non-S-RNase factors also are required for pollen rejection. As one approach to identifying such factors, we tested whether SC10-RNase from Nicotiana alata would bind to other stylar proteins in vitro. SC10-RNase was immobilized on Affi-gel, and binding proteins were analyzed by SDS-PAGE and immunoblotting. In addition to SC10-RNase and a small protein similar to lily chemocyanin, the most prominent binding proteins include NaTTS, 120K, and NaPELPIII, these latter three being arabinogalactan proteins previously shown to interact directly with pollen tubes. We also show that SC10-RNase and these glycoproteins migrate as a complex in a native PAGE system. Our hypothesis is that S-RNase forms a complex with these glycoproteins in the stylar ECM, that the glycoproteins interact directly with the pollen tubes and thus that the initial interaction between the pollen tube and S-RNase is indirect.