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Plant and Cell Physiology, 1997, Vol. 38, No. 3 243-247
© 1997

Import of Modified Dl Protein and its Assembly into Photosystem II by Isolated Chloroplasts

Guo-Jiang Wu and Akira Watanabe

Department of Biological Sciences, Graduate School of Science, University of Tokyo Hongo, Bunkyo-ku, Tokyo, 113 Japan

A portion of the rbcS gene that encoded the transit peptide and 20 amino acid residues of the N-tenninal region of the small subunit of ribulosebisphosphate carb-oxylase/oxygenase was fused to the 5' end of the psbA gene which encodes the Dl protein of PSII reaction center. The chimeric gene was expressed in vitro as a 42-kDa protein, which was imported into chloroplasts isolated from pea leaves. The imported protein was processed such that the transit peptide was lost in the stroma, the resultant protein was translocated into thylakoid membranes, and the C-ter-minal peptide was then removed to yield a mature protein with an N-terminal extension originated from the small sub-unit. The mature protein appeared to be assembled into the PSII core complex, resembling the native Dl protein in terms of protein structure and topology within the membrane. Our observations indicate that the structure of the precursor to the Dl protein includes information for the proper assembly of the protein into the PSII core complex.

(Received September 10, 1996; Revision received December 14, 1996. )
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