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Manipulation of protein-complex function by using an engineered heterotrimeric coiled-coil switch
https://nitech.repo.nii.ac.jp/records/5450
https://nitech.repo.nii.ac.jp/records/5450a47a401a-92ea-41bd-a07e-e35c4804b6e6
| 名前 / ファイル | ライセンス | アクション |
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本文_fulltext (437.0 kB)
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Org. Biomol. Chem., 2009, 7, 3102-3111-Reproduced by permission of The Royal Society of Chemistry (RSC)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||||||||||||||||||
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| 公開日 | 2012-11-06 | |||||||||||||||||||||||||
| タイトル | ||||||||||||||||||||||||||
| タイトル | Manipulation of protein-complex function by using an engineered heterotrimeric coiled-coil switch | |||||||||||||||||||||||||
| 言語 | en | |||||||||||||||||||||||||
| 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 |
Mizuno, Toshihisa
× Mizuno, Toshihisa
× Suzuki, Kumiko
× Imai, Tatsuya
× Kitade, Yuya
× Furutani, Yuji
× Kudo, Motonori
× Oda, Masayuki
× Kandori, Hideki
× Tsumoto, Kohei
× Tanaka, Toshiki
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| 著者別名 | ||||||||||||||||||||||||||
| 姓名 | 水野, 稔久 | |||||||||||||||||||||||||
| 著者別名 | ||||||||||||||||||||||||||
| 姓名 | 神取, 秀樹 | |||||||||||||||||||||||||
| 著者別名 | ||||||||||||||||||||||||||
| 姓名 | 田中, 俊樹 | |||||||||||||||||||||||||
| 書誌情報 |
en : Organic & biomolecular chemistry 巻 7, 号 15, p. 3102-3111, 発行日 2009-06-18 |
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| 出版者 | ||||||||||||||||||||||||||
| 出版者 | Royal Society of Chemistry | |||||||||||||||||||||||||
| 言語 | en | |||||||||||||||||||||||||
| ISSN | ||||||||||||||||||||||||||
| 収録物識別子タイプ | ISSN | |||||||||||||||||||||||||
| 収録物識別子 | 1477-0520 | |||||||||||||||||||||||||
| item_10001_source_id_32 | ||||||||||||||||||||||||||
| 収録物識別子タイプ | NCID | |||||||||||||||||||||||||
| 収録物識別子 | AA1168650X | |||||||||||||||||||||||||
| 出版タイプ | ||||||||||||||||||||||||||
| 出版タイプ | VoR | |||||||||||||||||||||||||
| 出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||||||||||||||||||||||
| item_10001_relation_34 | ||||||||||||||||||||||||||
| 関連タイプ | isIdenticalTo | |||||||||||||||||||||||||
| 識別子タイプ | DOI | |||||||||||||||||||||||||
| 関連識別子 | http://dx.doi.org/10.1039/b901118h | |||||||||||||||||||||||||
| 関連名称 | 10.1039/b901118h | |||||||||||||||||||||||||
| 内容記述 | ||||||||||||||||||||||||||
| 内容記述タイプ | Other | |||||||||||||||||||||||||
| 内容記述 | Design methodology of variant proteins, in which original functions can be manipulated by additive ligand binding, is an attractive target of protein engineering. Especially for multi-protein complexes, techniques for constructing variants which allow the switching on or off of original functions by ligands have been limited until now. We examined a method of utilizing a de novo designed protein module, IZ-DS, which has a tertiary structure that can be significantly changed from a random coil to a folded coiled-coil structure following binding with peptide ligand, IZ-3K. By introducing a metamorphosis IZ-DS sequence to one of the components in a target multi-protein complex, the IZ-3K binding and the subsequent structural transition of the IZ-DS moiety would affect the tertiary structure of the introduced protein unit, and the function of the total multi-protein complex may also be altered. In this research, we used the T7 RNA polymerase (T7 RNAP)/T7 lysozyme complex as the target multi-protein complex, in which allosteric binding of the T7 lysozyme to T7 RNAP halts the RNA synthesis of T7 RNAP. The IZ-DS sequence was introduced to the T7 lysozyme. By optimizing the introduction site of the IZ-DS sequence in the T7 lysozyme, we succeeded in constructing the T7 lysozyme variant, DS-Lys23. In the absence of IZ-3K, the mixture of T7 RNAP and DS-Lys23 exhibited RNA synthesis due to the weakening of the interaction between T7 RNAP and DS-Lys23. Whereas, after the addition of IZ-3K, RNA synthesis was significantly suppressed by the binding of DS-Lys23/IZ-3K complex. The present methodology using a designed ligand-dependent metamorphosis protein sequence constitutes another possible method for the de novo manipulation of various functions of natural protein complexes. | |||||||||||||||||||||||||
| 言語 | en | |||||||||||||||||||||||||
