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Updated: Jan 27, 2026

Light/dark Transition Test for Mice
Published on: November 13, 2006
Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a
Patricia A Austin1, I Stuart Ross, John D Mills
1Department of Biological Sciences, Keele University, Keele, Staffs, ST5 5BG, Staffs, UK.
Abstract:
Both short-term and long-term adaptations of cyanobacterial metabolism to light and dark were studied in Nostoc sp. Mac. Long-term adaptations were induced by growing cells in the presence of glucose under (a) 30 μE m-2 s-1 continuous white light, (b) under a 14/10 h light/dark cycle, or (c) complete darkness. Short-term regulation of enzyme activities by light was then studied in cells rendered osmotically fragile with lysozyme. Cells were briefly illuminated then enzyme activities were measured following rapid lysis in a hypotonic assay medium. The following results were obtained. (1) Relative to fresh weight, dark-grown cells contained less chlorophyll, much less phycoerythrin, but similar amounts of phycocyanin compared to cells grown under either light regime. Relative to chlorophyll, the higher phycocyanin and much lower phycoerythrin in the dark-grown vs light-grown cells resembles long term changes in pigment content that occur during complementary chromatic adaptation to red vs orange light. (2) Both dark and light/dark grown cells displayed generally lowered photosynthetic activities compared to light-grown cells. The exception to this was the activity of fructose 1,6-bisphosphatase, which was higher in dark-grown cells. However, the photosynthetic induction period was markedly shorter in the light/dark-grown cells indicating an adaptation to changing illumination during growth. (3) Inhibitor studies using methyl viologen show that the fructose 1,6-bisphosphatase is reversibly light-activated in vivo by the cyanobacterial thioredoxin system under all growth conditions. Glucose-6-phosphate dehydrogenase activity was detected in cells grown in all conditions and this activity was reversibly deactivated by light or by dithiothreitol. In contrast, the protonmotive ATPase F0F1-type ATPase was fully active in both light and dark-adapted cells regardless of the light regime used for growth. (4) It is concluded that the Calvin cycle enzymes, their short-term regulatory system, including thioredoxin, glucose-6-phosphate dehydrogenase and an F0F1 ATPase not under thioredoxin control, are expressed in cells grown in complete darkness. Adaptation to heterotrophic growth in this cyanobacterium does not appear to involve synthesis of different enzyme forms lacking thioredoxin control sequences.
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