Enzymes of choline synthesis in diverse plants: variation in phosphobase N-methyltransferase activities

Abstract

S-adenosyl-L-methionine dependent phospho-base N-methyltransferases are involved in the sequential methylations of phosphoethanolamine [Formula: see text] phosphomethylethanolamine [Formula: see text] phosphodimethylethanolamine [Formula: see text] phosphocholine. Phosphocholine is a precursor for the ubiquitous phospholipid phosphatidylcholine and for free choline, which can be oxidized to produce the osmoprotectant glycine betaine. Despite the importance of these enzymes to growth and stress tolerance, their activities have been studied in comparatively few plant species. Phospho-base N-methylating activities were assayed in leaf extracts prepared from 17 diverse plant species. All plants tested can perform the first step ( N-methylation of phosphoethanolamine) with in vitro activity rates varying from 0.13 nmol·min–1·g–1 fresh weight for soybean (Glycine max (L.) Merr.) and pea (Pisum sativum L.) to 25 nmol·min–1·g–1 fresh weight for cotton (Gossypium hirsutum L.). Of the plant species surveyed, only soybean and pea showed no capacity to perform the two subsequent N-methylation steps. Exposing plants to prolonged dark periods led to decreased phosphoethanolamine N-methylating activity relative to light-exposed controls with the extent of decrease varying among the species from 30% (Limonium perezii (Stapf) F.T. Hubb) to over 90% (Spinacia oleracea L., Beta vulgaris L., and Amaranthus caudatus L.). Thus, light-responsive properties and levels of phosphobase methyltransferase activities vary among plants with a trend towards higher activities being found in plants that accumulate glycine betaine.Key words: glycine betaine, choline, phosphatidylcholine, phosphocholine.