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Inhibition of the Formation of Photosynthetic Enzymes by Inhibitors of Photosynthesis
Author(s) -
Daniel McMahon,
Lawrence Bogorad
Publication year - 1968
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.43.2.188
Subject(s) - photosynthesis , enzyme , pyruvate carboxylase , chloramphenicol , isomerase , biochemistry , zea mays , rubisco , chemistry , c4 photosynthesis , ribulose , botany , biology , agronomy , antibiotics
It has been shown previously that an increase in ribulose diphosphate carboxylase activity occurs upon brief illumination of leaves of dark-grown Zea mays plants; an increase in ribose 5-phosphate isomerase occurs after prolonged illumination. Both of these responses to illumination are inhibited by chloramphenicol.The administration of p-chlorophenyldimethylurea, an inhibitor of photosynthesis, to etiolated maize does not affect the normal early rise in ribulose diphosphate carboxylase activity when the leaves are illuminated but does block the increase in ribose 5-phosphate isomerase. This pattern of response suggests that photosynthetic activity is required for the increase in isomerase-perhaps products of photosynthesis induce isomerase synthesis-but that the level of ribulose diphosphate carboxylase is controlled by other processes. Chlorophyll formation (as has been shown by others) is slightly suppressed by the inhibitor; levels of total soluble leaf protein appear to be unaffected.Salicylaldoxime, which is a more general inhibitor of metabolism than p-chlorophenyldimethylurea, arrests the normally observed increases of ribulose diphosphate carboxylase, ribose 5-phosphate isomerase, and chlorophyll during illumination of dark-grown maize. The level of soluble leaf protein is also lower in leaves treated with this compound.

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