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Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone

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J. Biol. Chem.-2018-Kawagoe-15095-106.pdf4.66 MBPDF見る/開く
この文献へのリンクには次のURLを使用してください:http://hdl.handle.net/2115/73070

タイトル: Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone
著者: Kawagoe, Soichiro 著作を一覧する
Nakagawa, Hiroshi 著作を一覧する
Kumeta, Hiroyuki 著作を一覧する
Ishimori, Koichiro 著作を一覧する
Saio, Tomohide 著作を一覧する
キーワード: molecular chaperone
prolyl isomerase
molecular dynamics
protein folding
structure-function
nuclear magnetic resonance (NMR)
hydrophobic interaction
peptidyl-prolyl isomerase domain
trigger factor
発行日: 2018年 9月28日
出版者: American Society for Biochemistry and Molecular Biology (ASBMB)
誌名: Journal of Biological Chemistry (JBC)
巻: 293
号: 39
開始ページ: 15095
終了ページ: 15106
出版社 DOI: 10.1074/jbc.RA118.003579
抄録: Molecular chaperones often possess functional modules that are specialized in assisting the formation of specific structural elements, such as a disulfide bridges and peptidyl-prolyl bonds in cis form, in the client protein. A ribosome-associated molecular chaperone trigger factor (TF), which has a peptidyl-prolyl cis/trans isomerase (PPIase) domain, acts as a highly efficient catalyst in the folding process limited by peptidyl-prolyl isomerization. Herein we report a study on the mechanism through which TF recognizes the proline residue in the unfolded client protein during the cis/trans isomerization process. The solution structure of TF in complex with the client protein showed that TF recognizes the proline-aromatic motif located in the hydrophobic stretch of the unfolded client protein through its conserved hydrophobic cleft, which suggests that TF preferentially accelerates the isomerization of the peptidyl-prolyl bond that is eventually folded into the core of the protein in its native fold. Molecular dynamics simulation revealed that TF exploits the backbone amide group of Ile(195) to form an intermolecular hydrogen bond with the carbonyl oxygen of the amino acid residue preceding the proline residue at the transition state, which presumably stabilizes the transition state and thus accelerates the isomerization. The importance of such intermolecular hydrogen-bond formation during the catalysis was further corroborated by the activity assay and NMR relaxation analysis.
Rights: This research was originally published in the Journal of Biological Chemistry. Authors. Soichiro Kawagoe, Hiroshi Nakagawa, Hiroyuki Kumeta, Koichiro Ishimori and Tomohide SaioTitle. J. Biol. Chem. 2018; Vol. 293, No. 39 : pp15095-pp15106. © 2018 Kawagoe et al.
資料タイプ: article
URI: http://hdl.handle.net/2115/73070
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 齋尾 智英

 

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