Zinc-Dependent Oligomerization of <i>Thermus thermophilus</i> Trigger Factor Chaperone
<i>Thermus thermophilus</i> trigger factor (<i>Tt</i>TF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn<sup>2+</sup>. However, little is known about the mechanism of zinc-dependent regulation of the <i>Tt</i>TF...
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| Autores principales: | , , , , |
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| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
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| Materias: | |
| Acceso en línea: | https://doaj.org/article/9387f760265d4623b412e62eef8a4b08 |
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| Sumario: | <i>Thermus thermophilus</i> trigger factor (<i>Tt</i>TF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn<sup>2+</sup>. However, little is known about the mechanism of zinc-dependent regulation of the <i>Tt</i>TF activity. Here we exploit in vitro biophysical experiments to investigate zinc-binding, the oligomeric state, the secondary structure, and the thermal stability of <i>Tt</i>TF in the absence and presence of Zn<sup>2+</sup>. The data show that full-length <i>Tt</i>TF binds Zn<sup>2+</sup>, but the isolated domains and tandem domains of <i>Tt</i>TF do not bind to Zn<sup>2+</sup>. Furthermore, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra suggested that Zn<sup>2+</sup>-binding induces the partial structural changes of <i>Tt</i>TF, and size exclusion chromatography-multi-angle light scattering (SEC-MALS) showed that Zn<sup>2+</sup> promotes <i>Tt</i>TF oligomerization. Given the previous work showing that the activity regulation of <i>E. coli</i> trigger factor is accompanied by oligomerization, the data suggest that <i>Tt</i>TF exploits zinc ions to induce the structural change coupled with the oligomerization to assemble the client-binding site, thereby effectively preventing proteins from misfolding in the thermal environment. |
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