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Phosphorylation of thylakoid proteins of Oryza sativa: in vitro characterization and effects of chilling temperatures

Journal Article · · Plant Physiol.; (United States)
DOI:https://doi.org/10.1104/pp.83.2.428· OSTI ID:6525996
The phosphorylation of thylakoid proteins of rice (Oryza sativa L.) was studied in vitro using (..gamma..-/sup 32/P)ATP. Several thylakoid proteins are labeled, including the light-harvesting complex of photosystem II. Protein phosphorylation is sensitive to temperature, pH, and ADP, ATP, and divalent cation concentrations. In the range pH 7 to 8.2, phosphorylation of the light-harvesting polypeptides declines above pH 7.5, whereas labeling of several other thylakoid polypeptides increases. Increasing divalent cation concentration from 3 to 20 millimolar results in a decrease in phosphorylation of the 26 kilodalton light-harvesting complex polypeptide and increased phosphorylation of several other polypeptides. ADP has an inhibitory effect on the phosphorylation of the light-harvesting complex polypeptides. Phosphorylation of the 26 kilodalton light-harvesting polypeptide requires 0.45 millimolar ATP for half-maximal phosphorylation, compared to 0.3 millimolar for the 32 kilodalton phosphoprotein. Low temperature inhibits the phosphorylation of thylakoid proteins in chilling-sensitive rice. However, phosphorylation of histones by thylakoid-bound kinase(s) is independent of temperature in the range of 25 to 5/sup 0/C.
Research Organization:
Advanced Genetic Sciences, Inc., Oakland, CA
OSTI ID:
6525996
Journal Information:
Plant Physiol.; (United States), Journal Name: Plant Physiol.; (United States) Vol. 83:2; ISSN PLPHA
Country of Publication:
United States
Language:
English