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Plant and Cell Physiology, 1982, Vol. 23, No. 4 575-583
© 1982

Article

Behavior of the 36,000-dalton Protein in the Internal Membranes of Squash Etioplasts during Greening

Masahiko Ikeuchi and Satoru Murakami

Department of Biology, College of General Education, University of Tokyo Komaba, Meguro-ku, Tokyo 153, Japan

The 36,000-dalton protein was found to be a major component in the internal membrane of etioplasts of dark-grown squash cotyledons by slab SDS-polyacrylamide gel electrophoresis. It was also a major membrane protein of the etioplast in other etiolated plants such as oat and maize. When the etioplasts were transformed into (etio)chloroplasts under continued illumination, depletion of the 36,000-dalton protein began without a lag time followed by their disappearance, while formation of apoproteins of the light-harvesting chlorophyll protein complex, 26,000- and 22,400-dalton proteins, was noted. A 55,000-dalton protein was also present and its content did not change during greening. O'Farrell's two-dimensional electrophoresis revealed that the 36,000-dalton protein consisted of at least four alkaline proteins of the same molecular weight but with different isoelectric points of 9.1, 8.8, 8.5 and 8.2. They were found to be very similar protein by partial proteolysis using staphylococcal protease. The two-dimensional electrophoresis pattern of the 36,000-dalton protein was altered after 1 hr illumination. These behaviors of the 36,000-dalton protein during the greening process were accompanied by transformation of the crystalline prolamellar body in the etioplast.

(Received September 16, 1981; Accepted March 15, 1982)
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