| Autor: |
Minho Keum, Dai Ito, Mi-Seong Kim, Yuxi Lin, Kyeong-Hyeon Yoon, Jihoon Kim, Sung-Hee Lee, Ji-Hun Kim, Wookyung Yu, Young-Ho Lee, Hyung-Sik Won |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
|
| Zdroj: |
Biology, Vol 10, Iss 11, p 1171 (2021) |
| Druh dokumentu: |
article |
| ISSN: |
2079-7737 |
| DOI: |
10.3390/biology10111171 |
| Popis: |
Hsp33, a prokaryotic redox-regulated holding chaperone, has been recently identified to be able to exhibit an unfoldase and aggregase activity against elongation factor Tu (EF-Tu) in its reduced state. In this study, we investigated the effect of elongation factor Ts (EF-Ts) and trigger factor (TF) on Hsp33-mediated EF-Tu unfolding and aggregation using gel filtration, light scattering, circular dichroism, and isothermal titration calorimetry. We found that EF-Tu unfolding and subsequent aggregation induced by Hsp33 were evident even in its complex state with EF-Ts, which enhanced EF-Tu stability. In addition, although TF alone had no substantial effect on the stability of EF-Tu, it markedly amplified the Hsp33-mediated EF-Tu unfolding and aggregation. Collectively, the present results constitute the first example of synergistic unfoldase/aggregase activity of molecular chaperones and suggest that the stability of EF-Tu is modulated by a sophisticated network of molecular chaperones to regulate protein biosynthesis in cells under stress conditions. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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