2015年7月
How Co-translational Folding of Multidomain Protein Is Affected by Elongation Schedule: Molecular Simulations
PLOS Computational Biology
- ,
- ,
- 巻
- 11
- 号
- 7
- 開始ページ
- e1004356
- 終了ページ
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1371/journal.pcbi.1004356
- 出版者・発行元
- PUBLIC LIBRARY SCIENCE
Co-translational folding (CTF) facilitates correct folding in vivo, but its precise mechanism remains elusive. For the CTF of a three-domain protein Sufl, it was reported that the translational attenuation is obligatory to acquire the functional state. Here, to gain structural insights on the underlying mechanisms, we performed comparative molecular simulations of SufI that mimic CTF as well as refolding schemes. A CTF scheme that relied on a codon-based prediction of translational rates exhibited folding probability markedly higher than that by the refolding scheme. When the CTF schedule is speeded up, the success rate dropped. These agree with experiments. Structural investigation clarified that misfolding of the middle domain was much more frequent in the refolding scheme than that in the codon-based CTF scheme. The middle domain is less stable and can fold via interactions with the folded N-terminal domain. Folding pathway networks showed the codon-based CTF gives narrower pathways to the native state than the refolding scheme.
- リンク情報
- ID情報
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- DOI : 10.1371/journal.pcbi.1004356
- ISSN : 1553-734X
- eISSN : 1553-7358
- ORCIDのPut Code : 18563608
- PubMed ID : 26158498
- Web of Science ID : WOS:000360620100025