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J. Biol. Chem., Vol. 261, Issue 24, 11138-11145, Aug, 1986

Regulation of chloroplast-encoded chlorophyll-binding protein translation during higher plant chloroplast biogenesis

RR Klein and JE Mullet

Etioplasts of 5-day-old dark-grown barley seedlings synthesize most of the soluble and membrane proteins found in chloroplasts of illuminated plants. Prominent among these proteins are the large subunit of ribulose bisphosphate carboxylase and the alpha- and beta-subunits of the chloroplast ATPase. However, etioplasts do not synthesize four chloroplast-encoded proteins which are major constituents of the chloroplast thylakoid membrane: two chlorophyll apoproteins of photosystem I (68 and 65 kDa) and two chlorophyll apoproteins of photosystem II (47 and 43 kDa). Pulse-labeling experiments show that the lack of radiolabel accumulation in the chlorophyll apoproteins in etioplasts is due to inhibition of synthesis rather than apoprotein instability. Illumination of 5-day-old dark-grown barley selectively induces synthesis of the plastid-encoded chlorophyll apoproteins and proteins of 32, 23, and 21 kDa. Synthesis of the chlorophyll apoproteins was significant in plants illuminated for 15 min and was near maximum by 1 h. The induction of photosystem I chlorophyll apoprotein synthesis was not accompanied by an increase in mRNA for these proteins. These results demonstrate that the synthesis of the plastid-encoded photosystem I chlorophyll apoproteins is blocked at the translational level in dark-grown barley. Translation of the chlorophyll apoproteins is induced rapidly by light with a time course which is similar to the light-dependent formation of chlorophyll from protochlorophyllide.
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