Regulation of ATP-sulfurylase and Adenosine 5'-phosphosulfate Sulfotransferase by the Sulfur and the Nitrogen Source in Heterotrophic Cell Suspension Cultures of Paul's Scarlet Rose
Publisher DOI
Abstract
The effect of the sulfur and the nitrogen source on the activity of adenosine 5'-phosphosulfate sulfotransferase (APSSTase) from cell suspension cultures of Rosa sp.(Paul's Scarlet rose) was studied.ATP-sulfurylase (EC 2.7.7.4), nitrate reductase (EC 1.6.6.1) and O-acetyl-L-serine sulfhydrylase (EC 4.2.99.9) were measured for comparison.APSSTase activity was increased by 200% after omission of a sulfur source and by 50% when cells were cultivated with NH4+ instead of NO3-.Lack of a nitrogen source or cultivation with H2S or cysteine as sulfur sources induced a decrease in APSST ase activity to a very low level.The decrease induced by H2S and cysteine was less pronounced in the presence of NH4+.ATP-sulfurylase was increased by 100% in cultures without a sulfur source, whereas lack of a nitrogen source or NH4+ instead of NO3- had no effect on its activity during 24 h.Cysteine decreased this enzyme activity by 40% after 24h.Taken together our results are consistent with the idea that APSSTase plays a central role in regulating sulfate assimilation and in coordinating it with nitrate assimilation, whereas A TP-sulfurylase seems to have an accessory function in these respects.
Date Issued
1986-10
Publication Type
Article
Subject(s)
Subjects
Rosa sp.
•
adenosine 5'-phosphosulfate sulfotransferase
•
ATP-sulfurylase
•
nitrate reductase
•
regulation of sulfate assimilation
Language(s)
en
Author(s)
Additional Credits
Journal
Journal of Plant Physiology
Publisher
Elsevier
ISSN
0176-1617
Access(Rights)
restricted