Trigger factor from Thermus thermophilus is a Zn2+-dependent chaperone.
The ribosome-associated chaperone trigger factor ( TF) of Escherichia coli interacts with a variety of newly synthesized polypeptides to assist their correct folding. Here, we report that the TF of thermophilic eubacterium, Thermus thermophilus, arrested spontaneous folding of green fluorescent protein by forming a 1:1 binary complex. The complex was isolable by gel-filtration but was shown to be dynamic because green fluorescent protein was released by alpha-casein in large excess. Unexpectedly, EDTA completely abolished the folding-arrest activity of TF, and analysis revealed that the TF from our preparation contained approximately 0.5 mol Zn2+/mol TF. The folding-arrest activity of TF that was saturated with Zn2+ (approximately 1 mol/mol TF) was twice as efficient as that of untreated TF. Thus, chaperone activity of thermophilic TF is Zn2+-dependent.[1]References
- Trigger factor from Thermus thermophilus is a Zn2+-dependent chaperone. Suno, R., Taguchi, H., Masui, R., Odaka, M., Yoshida, M. J. Biol. Chem. (2004) [Pubmed]
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