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Interaction between chloroplast and cytoplasmic factors in the inhibition of l ‐phenylalanine ammonia‐lyase activity
Author(s) -
Podstoiski Andrzej
Publication year - 1983
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1983.tb04151.x
Subject(s) - chloroplast , phenylalanine ammonia lyase , cytoplasm , biochemistry , chemistry , electron transport chain , enzyme , phenylalanine , photosynthesis , mitochondrion , amino acid , gene
Components of the system inactivating cytoplasmic l ‐phenylalanine ammonia‐lyase (PAL; EC 4.3.1.5.) in barley seedlings ( Hordeiim vulgare L. cv. Polon) were investigated. In vitro light‐activated chloroplasts and two cytoplasmic factors participate in the enzyme inhibition. One role of the chloroplasts is to mediate the reaction between PAL and the cytoplasmic factors, resulting in inactivation of the enzyme. Uncoupling (carbonyl cyanide m‐chlorophenyl hydrazone, valinomycin) or inhibiting [3‐(3,4‐dichlorophenyl)‐l,l‐dimethylurea] photosynthetic electron transport showed that electron transport is necessary to enable chloroplasts to mediate PAL inhibition. Preliminary results also indicate that mitochondria are able to mediate the inhibition. The role of this inhibiting system in the regulation of PAL activity in vivo is discussed.