Transit Peptides of Thylakoid Luminal Proteins : the Sites of Stromal Processing are Conserved among Higher Plants
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概要
- 論文の詳細を見る
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. β-turn/β-sheet/α-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.
- 日本植物生理学会の論文
著者
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WATANABE Akira
Research Center for Advanced Science and Technology, The University of Tokyo
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Konishi Tomokazu
Research Institute For Biochemical Regulation School Of Agricultural Sciences Nagoya University:(pre
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Maruta Yoshiyuki
Research Institute For Biochemical Regulation School Of Agricultural Sciences Nagoya University:(pre
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Shinohara Kenji
Molecular And Cell Biology Section Bio-resources Technology Division Forestry And Forest Products Re
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Shinohara Kenji
Molecular And Cell Biology Section Bio-resources Technology Division Forestry And Forest Products Re
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Watanabe Akira
Research Center For Advanced Science And Technology The University Of Tokyo
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