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エンドウ トシヤ
ENDO TOSHIYA
遠藤 斗志也 所属 京都産業大学 生命科学部 先端生命科学科 職種 客員教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 1992/07 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | THE CHLOROPLAST-TARGETING DOMAIN OF PLASTOCYANIN TRANSIT PEPTIDE CAN FORM A HELICAL STRUCTURE BUT DOES NOT HAVE A HIGH-AFFINITY FOR LIPID BILAYERS |
| 執筆形態 | その他 |
| 掲載誌名 | EUROPEAN JOURNAL OF BIOCHEMISTRY |
| 出版社・発行元 | SPRINGER VERLAG |
| 巻・号・頁 | 207(2),pp.671-675 |
| 著者・共著者 | T ENDO,K KAWAMURA,M NAKAI |
| 概要 | Conformational properties and interactions with lipid membranes were studied for the chemically synthesized peptides PC(1-37) and PC(1-43), corresponding to the N-terminal 37 and 43 residues, respectively, of the transit peptide of the precursor to plastocyanin of Silene pratensis. PC(1-43) covers the entire chloroplast targeting domain of the transit peptide. CD spectra of PC(1-37) and PC(1-43) showed that both peptides have little ordered structure in aqueous solutions but form partially helical conformations in the presence of detergent micelles or in methanol. Vesicle disruption and direct-binding experiments revealed, however, that neither PC(1-37) nor PC(1-43) had a high affinity for lipid membranes. Since in the intact plastocyanin transit peptide the chloroplast-targeting domain is followed by a hydrophobic thylakoid-transfer domain, the plastocyanin precursor may well be transported to the chloroplast surface first with the aid of the thylakoid-transfer domain. The chloroplast-targeting domain may then form a helical structure in the lipid environments, and a chloroplast-specific motif displayed on the helical structure may be recognized by a receptor protein located at the chloroplast envelope membranes. |
| ISSN | 0014-2956 |