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Oligomerization of a molecular chaperone modulates its activity
This item is licensed under:Creative Commons Attribution 4.0 International
| Title: | Oligomerization of a molecular chaperone modulates its activity |
| Authors: | Saio, Tomohide Browse this author →KAKEN DB | | Kawagoe, Soichiro Browse this author | | Ishimori, Koichiro Browse this author →KAKEN DB | | Kalodimos, Charalampos G. Browse this author |
| Issue Date: | 1-May-2018 |
| Publisher: | eLife Sciences Publications |
| Journal Title: | Elife |
| Volume: | 7 |
| Start Page: | 35731 |
| Publisher DOI: | 10.7554/eLife.35731.001 |
| Abstract: | Molecular chaperones alter the folding properties of cellular proteins via mechanisms that are not well understood. Here, we show that Trigger Factor (TF), an ATP-independent chaperone, exerts strikingly contrasting effects on the folding of non-native proteins as it transitions between a monomeric and a dimeric state. We used NMR spectroscopy to determine the atomic resolution structure of the 100 kDa dimeric TF. The structural data show that some of the substrate-binding sites are buried in the dimeric interface, explaining the lower affinity for protein substrates of the dimeric compared to the monomeric TF. Surprisingly, the dimeric TF associates faster with proteins and it exhibits stronger anti-aggregation and holdase activity than the monomeric TF. The structural data show that the dimer assembles in a way that substratebinding sites in the two subunits form a large contiguous surface inside a cavity, thus accounting for the observed accelerated association with unfolded proteins. Our results demonstrate how the activity of a chaperone can be modulated to provide distinct functional outcomes in the cell. |
| Rights: | https://creativecommons.org/licenses/by/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/71490 |
| Appears in Collections: | 理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 齋尾 智英
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