To investigate if pollen possesses glyoxysomal function, we analyzed the activities of isocitrate lyase and malate synthase genes. Because the activities of these enzymes were exceedingly low in pollen extracts, we constructed fusion genes encoding j3-glucuronidase (CUS) that are regulated by isocitrate lyase or malate synthase promoters from Brassica napus L. to increase the sensitivity of our assays. Expression of the fusion genes in transgenic tobacco was qualitatively similar to that of the endogenous genes; CUS activity was low in dry seeds, maximal in seedlings, and very low or undetectable in leaves, indicating that the promoters are regulated correctly. We showed that isocitrate lyase and malate synthase genes are active at specific stages of pollen development and that their activities are not enhanced during pollen germination in transgenic tobacco. We also confirmed that the endogenous genes are active by showing that the corresponding mRNAs could be detected in pollen at specific stages of development. The activation of the isocitrate lyase and malate synthase genes suggests that glyoxysomal function is induced during pollen development.Glyoxysomes are specialized peroxisomes that play a pivotal role in the postgerminative growth of oilseed plants (Beevers, 1979;Huang et al., 1983;Trelease and Doman, 1984). These organelles contain the glyoxylate cycle and /3-oxidation enzymes that catalyze the net conversion of fatty acids into succinate and, thus, account for the ability of plants to utilize lipids as a carbon source for carbohydrate synthesis. The carbohydrates generated as a result of these reactions serve as nutrients for seedlings until they become photosynthetically active.Glyoxysomal function is induced at several stages of the plant life cycle when peroxisomes with different metabolic roles are converted into glyoxysomes. The induction of glyoxysomal function is generally monitored using two key glyoxylate cycle enzymes, isocitrate lyase and malate synthase, which are required for glyoxysomal function and are associated exclusively with glyoxysomes (reviewed by Olsen and