WEKO3
アイテム
Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure
https://repository.lib.tottori-u.ac.jp/records/7244
https://repository.lib.tottori-u.ac.jp/records/7244b7d304b6-bfac-45b1-8a9c-388142e7dcf4
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
jbc294(5)_1590.pdf (4.3 MB)
|
|
| Item type | 学術雑誌論文 / Journal Article(1) | |||||
|---|---|---|---|---|---|---|
| 公開日 | 2022-07-20 | |||||
| タイトル | ||||||
| タイトル | Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| キーワード | ||||||
| 主題 | molecular chaperone | |||||
| キーワード | ||||||
| 主題 | protein folding | |||||
| キーワード | ||||||
| 主題 | Gram-negative bacteria | |||||
| キーワード | ||||||
| 主題 | protein aggregation | |||||
| キーワード | ||||||
| 主題 | small heat shock protein (sHsp) | |||||
| キーワード | ||||||
| 主題 | amyloid | |||||
| キーワード | ||||||
| 主題 | acid denaturation | |||||
| キーワード | ||||||
| 主題 | periplasm | |||||
| キーワード | ||||||
| 主題 | protein fibrillogenesis | |||||
| キーワード | ||||||
| 主題 | reversible fibrillation | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | molecular chaperone | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | protein folding | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | Gram-negative bacteria | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | protein aggregation | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | small heat shock protein (sHsp) | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | amyloid | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | acid denaturation | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | periplasm | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | protein fibrillogenesis | |||||
| キーワード | ||||||
| 言語 | en | |||||
| 主題 | reversible fibrillation | |||||
| 資源タイプ | ||||||
| 資源タイプ | journal article | |||||
| 著者 |
本郷, 邦広
× 本郷, 邦広× 河田, 康志× 溝端, 知宏× Miyawaki, Shiori× Uemura, Yumi |
|||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Graduate School of Sustainability Science, Tottori University | |||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Department of Engineering, Tottori University | |||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Graduate School of Sustainability Science, Tottori University / Department of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University | |||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Graduate School of Sustainability Science, Tottori University / Department of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University | |||||
| 著者所属（英） | ||||||
| 言語 | en | |||||
| 値 | Graduate School of Sustainability Science, Tottori University / Department of Engineering, Tottori University / Center for Research on Green Sustainable Chemistry, Tottori University | |||||
| 抄録 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | The periplasmic small heat shock protein HdeA from Escherichia coli is inactive under normal growth conditions (at pH 7) and activated only when E. coli cells are subjected to a sudden decrease in pH, converting HdeA into an acid-denatured active state. Here, using in vitro fibrillation assays, transmission EM, atomic-force microscopy, and CD analyses, we found that when HdeA is active as a molecular chaperone, it is also capable of forming inactive aggregates that, at first glance, resemble amyloid fibrils. We noted that the molecular chaperone activity of HdeA takes precedence over fibrillogenesis under acidic conditions, as the presence of denatured substrate protein was sufficient to suppress HdeA fibril formation. Further experiments suggested that the secondary structure of HdeA fibrils deviates somewhat from typical amyloid fibrils and contains α-helices. Strikingly, HdeA fibrils that formed at pH 2 were immediately resolubilized by a simple shift to pH 7 and from there could regain molecular chaperone activity upon a return to pH 1. HdeA, therefore, provides an unusual example of a “reversible” form of protein fibrillation with an atypical secondary structure composition. The competition between active assistance of denatured polypeptides (its “molecular chaperone” activity) and the formation of inactive fibrillary deposits (its “fibrillogenic” activity) provides a unique opportunity to probe the relationship among protein function, structure, and aggregation in detail. | |||||
| 書誌情報 |
JOURNAL OF BIOLOGICAL CHEMISTRY en : JOURNAL OF BIOLOGICAL CHEMISTRY 巻 294, 号 5, p. 1590-1601, 発行日 2019-02-01 |
|||||
| 出版者 | ||||||
| 出版者 | American Society for Biochemistry and Molecular Biology | |||||
| ISSN | ||||||
| 収録物識別子タイプ | ISSN | |||||
| 収録物識別子 | 00219258 | |||||
| DOI | ||||||
| 関連タイプ | isIdenticalTo | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | 10.1074/jbc.RA118.005611 | |||||
| 権利 | ||||||
| 権利情報 | © 2019 Miyawaki et al. Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc. | |||||
| 情報源 | ||||||
| 関連名称 | Miyawaki Shiori, Uemura Yumi, Hongo Kunihiro, et al. Acid-denatured small heat shock protein HdeA from Escherichia coli forms reversible fibrils with an atypical secondary structure. JOURNAL OF BIOLOGICAL CHEMISTRY. 2019. 294(5). 1590-1601. doi:10.1074/jb | |||||
| 関連サイト | ||||||
| 識別子タイプ | URI | |||||
| 関連識別子 | https://www.sciencedirect.com/science/article/pii/S0021925820364681 | |||||
| 関連名称 | https://www.sciencedirect.com/science/article/pii/S0021925820364681 | |||||
| 著者版フラグ | ||||||
| 出版タイプ | VoR | |||||
| EISSN | ||||||
| 値 | 1083351X | |||||
