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Simple Summary  Metal ions often play important roles in biological processes.  Thermus thermophilus  trigger factor ( Tt TF) is a zinc-dependent molecular chaperone where Zn 2+  has been shown to enhance its folding-arrest activity. However, the mechanisms of how Zn 2+  binds to  Tt TF and how Zn 2+  affects the activity of  Tt TF are yet to be elucidated. As a first step in understanding the mechanism, we performed in vitro biophysical experiments on  Tt TF to investigate the zinc-binding site on  Tt TF and unveil how Zn 2+  alters the physical properties of  Tt TF, including secondary structure, thermal stability, and oligomeric state. Our results showed that  Tt TF binds Zn 2+  in a 1:1 ratio, and all three domains of  Tt TF are involved in zinc-binding. We found that Zn 2+  does not affect the thermal stability of  Tt TF, whereas it does induce partial structural change and promote the oligomerization of  Tt TF. Given that the folding-arrest activity of  Escherichia coli  TF ( Ec TF) is regulated by its oligomerization, our results imply that  Tt TF exploits Zn 2+  to modulate its oligomeric state to regulate the activity.    Abstract   Thermus thermophilus  trigger factor ( Tt TF) is a zinc-dependent molecular chaperone whose folding-arrest activity is regulated by Zn 2+ . However, little is known about the mechanism of zinc-dependent regulation of the  Tt TF activity. Here we exploit in vitro biophysical experiments to investigate zinc-binding, the oligomeric state, the secondary structure, and the thermal stability of  Tt TF in the absence and presence of Zn 2+ . The data show that full-length  Tt TF binds Zn 2+ , but the isolated domains and tandem domains of  Tt TF do not bind to Zn 2+ . Furthermore, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra suggested that Zn 2+ -binding induces the partial structural changes of  Tt TF, and size exclusion chromatography-multi-angle light scattering (SEC-MALS) showed that Zn 2+  promotes  Tt TF oligomerization. Given the previous work showing that the activity regulation of  E. coli  trigger factor is accompanied by oligomerization, the data suggest that  Tt 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.

Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone