Two-dimensional patterns of soluble proteins including three hydrolytic enzymes of mature pollen of tristylous Lythrum salicaria

Abstract

Lythrum salicaria, now a widespread invasive species, exhibits tristyly, a form of heteromorphic selfincompatibility. In tristyly, each plant exhibits one (and only one) of three morphologically different floral forms. Moreover, each flower produces two types of stamens, and these two exhibit different incompatibility reactions. Differences between stamens of a single flower must be the result of epigenetic phenomena and for that reason, we performed two-dimensional gel electrophoresis (2-DE) to analyze fractions of soluble proteins derived from the pollen coat and protoplast including three hydrolytic enzymes from the six different stamen types (two from each of three floral forms). There were significant differences in the 2-D protein profiles both between pollen from the same flower and between the same type of pollen from two different flowers, in the pollen coat as well as in the protoplast extracts. In five of the six samples of pollen fractions, characteristic peptides were found. Quantitative differences between pollen from the same flower were observed in case of esterases. Furthermore, analysis of proteases and acid phosphatases revealed also qualitative differences between these enzymes in pollen from the same flower.