Phosphorylation of proteins in the stem section of etiolated rice seedling irradiated with red light.

The molecular mechanism of light signal perception was analyzed using stem sections of etiolated rice (Oryza sativa L.) seedlings irradiated with red light from a fluorescent lamp. The membrane and cytosol fractions were labeled by 40 nM [gamma-32P]ATP for 10 s at 0 degrees C and proteins were separated by two-dimensional polyacrylamide gel electrophoresis. Phosphorylation of three proteins with molecular weights of 16, 17 and 18 kDa in the rice increased with the intensity of red light irradiation (50 micromol/m2/s) for 16 min. Most of the phosphorylation activity was present in the cytosol fraction. The three proteins cross-reacted with the anti-nucleoside diphosphate (NDP) kinase antibody. Phosphorylation of these proteins was correlated with changes in the activity of NDP kinase. These proteins phosphorylated histone III-S, a substrate for measuring the protein kinase activity. By phospho-amino acid analysis, phosphoserine was found present in the phosphorylated proteins. These rapidly phosphorylated proteins would thus appear to have the features of NDP kinase.