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THE PLANT CELL, Vol 8, Issue 4 713-724, Copyright © 1996 by American Society of Plant Biologists
Increased Phosphorylation of a 26-kD Pollen Protein Is Induced by the Self-Incompatibility Response in Papaver rhoeas
J. J. Rudd, FCH. Franklin, J. M. Lord and V. E. Franklin-Tong
Wolfson Laboratory for Plant Molecular Biology, School of Biological Sciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT United Kingdom
We have investigated whether specific protein phosphorylation events are
induced in Papaver rhoeas pollen as a consequence of the
self-incompatibility (SI) response. Pollen grown in vitro in the presence
of 32P-orthophosphate was challenged with biologically active recombinant S
proteins, and pollen proteins were extracted and analyzed. The results
provide strong evidence that the increased phosphorylation of a 26-kD
protein of pl 6.2, p26, is specifically induced by the SI response. This
phosphorylation event occurs in living pollen tubes and was observed
specifically when pollen was challenged with S proteins that are
incompatible with the S alleles carried by the pollen and not when pollen
was challenged with compatible or incompatible heat-denatured S proteins.
Further characterization demonstrated that p26 comprises two
phosphoproteins, p26.1 and p26.2, that are found in soluble and microsomal
fractions, respectively. Increased phosphorylation of p26.1 is implicated
in the SI response and appears to be Ca2+ and calmodulin dependent. These
data argue for the involvement of a Ca2+-dependent protein kinase requiring
calmodulin-like domains, whose activation comprises an intracellular signal
mediating the SI response in P. rhoeas pollen.
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