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Plant and Cell Physiology, 1985, Vol. 26, No. 5 839-846
© 1985

Article

Detection of a Precursor Polypeptide of the Rapidly-Synthesized 32,000-Dalton Thylakoid Protein in Spinach Chloroplasts

Ei-ichi Minami and Akira Watanabe

Research Institute for Biochemical Regulation, Faculty of Agriculture, Nagoya University Chikusa-ku, Nagoya 464, Japan

Spinach chloroplast RNA was translated in a wheat germ cell-free system in the presence of [35S]methionine or [3H]lysine, and the products were analyzed by SDS polyacrylamide gel electrophoresis and fluorography. A polypeptide with molecular mass of 2,000-Da larger than the 32,000-Da thylakoid protein was detected as a major product labeled by [35S]methionine but not by [3H]lysine. Peptide mapping of this polypeptide showed a pattern very close to that of the 32,000-Da protein synthesized in isolated chloroplasts. A better separation of this polypeptide from the 32,000-Da protein was observed in the electrophoresis on polyacrylamide gel including urea at 8 M. Pulse-labeling of the isolated chloroplasts showed the occurrence of the larger molecular weight form, which was converted to the mature size by a chasing incubation with cold methionine. These results suggested that the 32,000-Da protein of spinach is translated primarily as a high molecular weight precursor in the chloroplasts, as has been reported for other plant species.

(Received March 30, 1985; Accepted April 23, 1985)
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