Regulation of Sulfate Assimilation by Light and O-Acetyl-l-Serine in Lemna minor L.
Open Access
- 1 September 1991
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 97 (1) , 253-258
- https://doi.org/10.1104/pp.97.1.253
Abstract
The effect of 0.5 millimolar O-acetyl-l-serine added to the nutrient solution on sulfate assimilation of Lemna minor L., cultivated in the light or in the dark, or transferred from light to the dark, was examined. During 24 hours after transfer from light to the dark the extractable activity of adenosine 5′-phosphosulfate sulfotransferase, a key enzyme of sulfate assimilation, decreased to 10% of the light control. Nitrate reductase (EC 1.7.7.1.) activity, measured for comparison, decreased to 40%. Adenosine 5′-triphosphate (ATP) sulfurylase (EC 2.7.7.4.) and O-acetyl-l-serine sulfhydrylase (EC 4.2.99.8.) activities were not affected by the transfer. When O-acetyl-l-serine was added to the nutrient solution at the time of transfer to the dark, adenosine 5′-phosphosulfate sulfotransferase activity was still at 50% of the light control after 24 hours, ATP sulfurylase and O-acetyl-l-serine sulfhydrylase activity were again not affected, and nitrate reductase activity decreased as before. Addition of O-acetyl-l-serine at the time of the transfer caused a 100% increase in acid-soluble SH compounds after 24 hours in the dark. In continuous light the corresponding increase was 200%. During 24 hours after transfer to the dark the assimilation of 35SO42− into organic compounds decreased by 80% without O-acetyl-l-serine but was comparable to light controls in its presence. The addition of O-acetyl-l-serine to Lemna minor precultivated in the dark for 24 hours induced an increase in adenosine 5′-phosphosulfate sulfotransferase activity so that a constant level of 50% of the light control was reached after an additional 9 hours. Cycloheximide as well as 6-methyl-purine inhibited this effect. In the same type of experiment O-acetyl-l-serine induced a 100-fold increase in the incorporation of label from 35SO42− into cysteine after additional 24 hours in the dark. Taken together, these results show that exogenous O-acetyl-l-serine has a regulatory effect on assimilatory sulfate reduction of L. minor in light and darkness. They are in agreement with the idea that this compound is a limiting factor for sulfate assimilation and seem to be in contrast to the proposed strict light control of sulfate assimilation.Keywords
This publication has 10 references indexed in Scilit:
- Expression of Leaf Nitrate Reductase Genes from Tomato and Tobacco in Relation to Light-Dark Regimes and Nitrate SupplyPlant Physiology, 1988
- The determination of glutathione, cyst(e)ine, and other thiols and disulfides in biological samples using high-performance liquid chromatography with dual electrochemical detectionAnalytical Biochemistry, 1987
- Protein Degradation in Lemna with Particular Reference to Ribulose Bisphosphate CarboxylasePlant Physiology, 1987
- Regulation of Sulfate Assimilation by Nitrogen Nutrition in the Duckweed Lemna minor L.Plant Physiology, 1984
- Role of O-Acetylserine in Hydrogen Sulfide Emission from Pumpkin Leaves in Response to SulfatePlant Physiology, 1983
- Sulfur Deprivation and Nitrogen Metabolism in Maize SeedlingsPlant Physiology, 1978
- Regulation of adenosine triphosphate sulfurylase in cultured tobacco cells. Effects of sulfur and nitrogen sources on the formation and decay of the enzyme.Journal of Biological Chemistry, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- An Aspergillus nidulans mutant lacking cystathionine β-synthase: Identity of L-serine sulfhydrylase with cystathionine β-synthase and its distinctness from O-acetyl-L-seline sulfhydrylaseBiochimica et Biophysica Acta (BBA) - General Subjects, 1973
- Regulation of L-cysteine biosynthesis in Salmonella typhimurium. I. Effects of growth of varying sulfur sources and O-acetyl-L-serine on gene expression.1971