WEKO3
インデックスリンク
アイテム
Isolation of a Drosophila gene coding for a protein containing a novel phosphatidylserine-binding motif
http://hdl.handle.net/2297/14553
http://hdl.handle.net/2297/145538db61242-e0e5-4a1a-b527-e93c8370e5c0
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
PH-PR-NAKANISHI-Y-593.pdf (387.7 kB)
|
|
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2017-10-04 | |||||
| タイトル | ||||||
| タイトル | Isolation of a Drosophila gene coding for a protein containing a novel phosphatidylserine-binding motif | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
| 資源タイプ | journal article | |||||
| 著者 |
Nakai, Yuji
× Nakai, Yuji× Nomura, Yoshitaka× Sato, Toshihiro× Shiratsuchi, Akiko× Nakanishi, Yoshinobu |
|||||
| 提供者所属 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 金沢大学医薬保健研究域薬学系 | |||||
| 書誌情報 |
Journal of Biochemistry 巻 137, 号 5, p. 593-599, 発行日 2005-05-01 |
|||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 0021-924X | |||||
| NCID | ||||||
| 収録物識別子タイプ | NCID | |||||
| 収録物識別子 | AA00694073 | |||||
| DOI | ||||||
| 関連タイプ | isIdenticalTo | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1093/jb/mvi072 | |||||
| 出版者 | ||||||
| 出版者 | 日本生化学会 = Japanese Biochemical Society | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | To elucidate the molecular basis of the binding of proteins to the membrane phospholipid phosphatidylserine (PS), we characterized PS-binding peptides isolated from a phage display library. Amino acid sequences deduced from the nucleotide sequences of over 60 phage clones isolated revealed that there was no common primary structure among these peptides, but all peptides were rich in basic amino acid residues. In particular, 15 clones encoded peptides that contained contiguous arginine residues. Characterization of two such peptides in more detail showed that they bound to PS, and to a much lower extent to other phospholipids, including phosphatidylinositol, phosphatidylethanolamine, and phosphatidylcholine. Unlike other Ca2+-dependent PS-binding proteins, these peptides did not require Ca2+ for binding to PS, and the addition of Ca2+ did not alter the phospholipid specificity. Substitution of one of the two RR sequences in one peptide by alanine had no effect, but that of both sequences completely abolished the activity. Furthermore, we identified a Drosophila gene coding for a presumed nuclear protein that shares an amino acid sequence, including a RR residue, with one of the two PS-binding peptides. This protein bound to PS partly depending on the presence of the RR residue. These results allowed us to conclude that an amino acid sequence including contiguous arginine residues is a novel motif that defines Ca2+-independent PS-binding activity. © 2005 The Japanese Biochemical Society. | |||||
| 権利 | ||||||
| 権利情報 | Copyright © 2005 Japanese Biochemical Society | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
| 関連URI | ||||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | http://dx.doi.org/10.1093/jb/mvi072 | |||||
| 関連URI | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | http://jb.oxfordjournals.org/cgi/content/abstract/137/5/593 | |||||
