Phosphorylation of pollen proteins in relation to self-incompatibility in rye (Secale cereale L.) |
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Authors: | P. Wehling B. Hackauf G. Wricke |
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Affiliation: | (1) Institute of Applied Genetics, Herrenhäuser Str. 2, D-30419 Hannover, Germany |
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Abstract: | The gametophytic two-locus self-incompatibility (SI) system in rye was investigated in view of a possible involvement of protein phosphorylation and Ca2+ as constituents of a signal transduction mechanism. Phosphorylation kinetics in pollen grains was found to be significantly different after in vitro treatment of pollen with either cross or self stigma proteins, with a pronounced phosphorylation activity in self-treated pollen grains. Loss of SI in self-compatible (SC) mutants was associated with a significantly decreased basic phosphorylation activity in untreated pollen grains as compared to SI genotypes. Separation of phosphorylated pollen proteins by SDS-PAGE reveals four major proteins in the MW range of 43–82 kDa which were differently phosphorylated in SI vs SC genotypes as well as in cross vs self-treated pollen grains. Application of different protein kinase inhibitors and the Ca2+ antagonists verapamil and La3+ to isolated stigmas resulted in an inhibition of the SI response in in vitro self-pollination. The role of protein kinases and Ca2+ as constituents of a putative SI-specific signal transduction mechanism is discussed. |
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Keywords: | Secale cereale L. Self-incompatibility Protein kinases Self-fertile mutants Signal transduction |
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