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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Planta 136 (1977), S. 181-186 
    ISSN: 1432-2048
    Keywords: Enzyme Regulation ; Sinapis alba ; Phytochrome ; Phenylalanine ammonia-lyase ; Ribulosebisphosphate carboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phytochrome controls the appearance of many enzymes in the mustard (Sinapis alba L.) cotyledons. The problem has been whether the effect of phytochrome on the appearance of enzymes in this organ is due to a common initial action of Pfr, e.g. due to the liberation of a “second messenger”. We have compared the modulation by light (phytochrome) of the appearance of phenylalanine ammonia lyase (PAL)+ and ribulosebisphosphate carboxylase (Carboxylase)+. PAL becomes detectable in the mustard cotyledons at 27 h after sowing while Carboxylase starts to appear only at 42 h after sowing (starting points, 25° C). The starting points cannot be shifted by light. As a major result, in the case of PAL the inductive effect of continuous red light (given from the time of sowing) remains fully reversible by 756 nm-light up to the starting point (27 h after sowing) while with Carboxylase full reversibility in continuous red light is lost at approximately 15 h after sowing. While the induction of Carboxylase is already saturated at a very low level of Pfr (e.g. continuous 756 nm-light saturates the response) and does not depend on irradiance (e.g. continuous 675 mW m-2 red light and 67.5 mW m-2 red light lead to the same time course), PAL induction is a graded response over a wide range of Pfr doses and depends strongly on the fluence rate (high irradiance response, HIR). It is concluded that PAL induction and Carboxylase induction are not only separated in time but differ in every regard except that both responses are mediated by phytochrome. The present data support the previous conclusion that the specification of the temporal and spatial pattern of development is independent of phytochrome even though the realization of the pattern of development can only occur in the presence of phytochrome (Pfr). It seems that there is no feedback from pattern realization to pattern specification.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-2048
    Keywords: Carotenoids ; Chlorophylls ; Herbicides ; Phytochrome ; Plastid development ; Ribulosebisphosphate carboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Treatment of the mustard (Sinapis alba L.) seedling with the herbicide SAN 9789 inhibits synthesis of colored carotenoids and interferes with the formation of plastid membrane lipids without affecting growth and morphogenesis significantly. In farred light, which is hardly absorbed by chlorophyll, development of plastid ultrastructure, synthesis of ribulosebisphosphate carboxylase and synthesis of chlorophyll are not affected by SAN 9789. It is concluded that normal phytochrome actions on plastid structural development, protein and chlorophyll syntheses are not affected by the absence of carotenoids provided that there is no significant light absorption in chlorophyll. The findings show that the inhibition of synthesis of one set of plastid membrane components (the carotenoids) does not stop synthesis of other components such as chlorophyll and does not halt membrane assembly. Supplementary experiments with the closely related compound SAN 9785, which affects the amount and composition of plastid lipids but not carotenoid and chlorophyll syntheses, suggest that the effect of the herbicide SAN 9789 is due exclusively to its inhibition of synthesis of colored carotenoids. In the presence of SAN 9789 white or red light at high fluence rate causes photodestruction of chlorophyll and ribulosebisphosphate carboxylase and photodecomposition of thylakoids. These effects are interpreted as resulting exclusively from the self-photooxidation and photosensitizing action of chlorophyll once the protection by carotenoids of chlorophyll against self- and sensitized photooxidation is lost.
    Type of Medium: Electronic Resource
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