Nucleoside diphosphate kinase isoforms regulated by phytochrome A isolated from oat coleoptiles.

Abstract

Nucleoside diphosphate kinase (NDPK) (EC 2.7.4.6), the enzyme transferring the phosphate residue from ATP to nucleoside diphosphates, is localized mainly in the cytoplasm and mitochondria and in smaller amounts in cell nuclei and the microsomal fraction. Exposure of etiolated oat seedlings to red light causes an increase of the enzyme activity by about 42% in nuclear fraction, 7% in etioplastic and 14% in postetioplastic fraction. Endogenous phytochrome A, as visualized by an immunochemical method, translocates from the cytoplasm into the nucleus upon red, far-red or white light activation. Nuclei purified from oat seedlings contain two, and the postnuclear fraction four easily separated forms of NDPK. One of the nuclear isoforms (I(n)) and one isoform isolated from the postnuclear fraction (II(pn)) are activated by red light in the presence of phytochrome A purified from etiolated oat coleoptiles. Both phytochrome A-activated NDPKs purified to electrophoretic homogeneity have the same molecular mass (17-18 kDa) determined by SDS/PAGE. Both enzymes in the native form have similar molecular masses (71 and 63 kDa).