On the Regulation of Enzyme Levels (phenylalanine ammonia-lyase) in Different Organs of a Plant (Sinapis alba L.)

Abstract

The time courses of formation of the enzyme phenylalanine ammonia-lyase (PAL; EC 4.3.1.5) mediated by far-red light (i. e. by phytochrome, Pfr) in cotyledons and hypocotyl of the mustard seedling (Sinapis alba L.) are described. While PAL activity in the cotyledons can scarcely be detected in the dark-grown seedling, the enzyme can be synthesized in the hypocotyl even in the dark. However, the degree of induction by far-red light is much greater in the cotyledons than in the hypocotyl. In the cotyledons the enzyme is not stable. The enzyme level eventually returns to nearly zero even under continuous far-red light. The time course of the level of PAL in the cotyledons (Fig. 1) can be explained by the following 3 factors (Fig. 2): 1. Induction of PAL synthesis by Pfr, whereby Pfr is continuously required; 2. Inactivation (degradation) of PAL by an inactivating principle; 3. Repression of PAL synthesis. The time course of the level of PAL in the hypocotyl is completely different (Fig. 1). An explanation of the hypocotyl data is presented which is based on the assumption that PAL synthesis in the dark and PAL synthesis mediated by phytochrome are independent phenomena which occur in different tissues of the hypocotyl. It appears that the occurrence of dark synthesis of a stable enzyme in the hypocotyl explains the seemingly dramatic difference between the cotyledons and the hypocotyl with respect to PAL.