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Plant and Cell Physiology, 1993, Vol. 34, No. 7 1081-1087
© 1993

Transit Peptides of Thylakoid Luminal Proteins: the Sites of Stromal Processing are Conserved among Higher Plants

Tomokazu Konishi1,3, Yoshiyuki Maruta1,4, Kenji Shinohara2 and Akira Watanabe1

1Research Institute for Biochemical Regulation, School of Agricultural Sciences, Nagoya University Chikusa-ku, Nagoya, 464-01 Japan
2Molecular and Cell Biology Section, Bio-Resources Technology Division, Forestry and Forest Products Research Institute Inashiki, Ibaraki, 305 Japan

The amino terminal of the transport intermediate of the 23-kDa protein of PSII, which was generated by stromal processing, was determined by radiosequencing in order to identify the site of processing of its precursor. The site was located in the central region of the transit peptide. The primary structure of the processing site included a motif that is common to the processing sites of transit peptides of various stromal proteins. This common motif was also found in the transit peptides of other thylakoid luminal proteins, an indication of its conservation among higher plants. A common secondary structure, rßturn/rß-sheet/{alpha}-helix, was predicted from the amino acid sequence around the consensus motif. This structural similarity between stromal and thylakoid luminal proteins suggests that the sequences are under a common selective pressure to maintain these sites of cleavage by a stromal processing peptidase.

3Present address: Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Kyoto, 606-01 Japan

4Present address: Plant Breeding and Genetics Research Laboratory, Japan Tobacco Company, Toyota-cho, Iwata, Shizuoka, 438 Japan

(Received February 26, 1993; Accepted August 11, 1993)
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