Thermosome: A Group II Chaperonin of Archaea

Abstract

Chaperonin, heat shock protein 60, plays an important role in the proteostasis of cytosol. Chaperonins are divided into two groups: group I and group II. Group II chaperonins exist in eukaryotes and archaea, and these chaperonins are named CCT/TRiC and Thermosome, respectively. Group II chaperonins have almost the same structure as group I chaperonins. The main difference is the existence of a helical protrusion, which constitutes a built‐in lid of the cavity. Group II chaperonin captures an unfolded protein in the cavity in the open conformation and changes to the closed conformation in an ATP‐dependent manner, which triggers folding of the captured protein. As Thermosome is relatively stable and simple compared with CCT, the conformational change mechanism and also the interaction with co‐chaperone, Prefoldin, have been studied in detail using Thermosome. The conformational change procedure of Thermosome will give insights on protein folding mechanism by group II chaperonins.

Key Concepts

  • Group II chaperonin is an essential cytosolic molecular chaperone in eukaryotes and archaea.
  • The archaeal group II chaperonin is named Thermosome.
  • Group II chaperonin has a built‐in lid for the central cavity.
  • As ATP induces a conformational change from the open to the closed conformation, twisting of the ring occurs.
  • Group II chaperonin cooperates with a co‐chaperone, Prefoldin, which captures an unfolded protein and transfers it to the central cavity of the group II chaperonin.

Keywords: Hsp60; chaperone; chaperonin; Thermosome; conformational change; protein folding; ATPase

Figure 1. Structure of Thermosome in closed and open conformation. The images were generated by PyMol (https://www.pymol.org/) using the PDB data (closed (1Q3Q) and open (lidless) (3IYF).
Figure 2. Rotational motion of group II chaperonin observed by diffracted X‐ray tracking. Reproduced from Sekiguchi et al. (2013) © PLoS One.
Figure 3. Schematic protein folding cycle model of group II chaperonin. Only one ring is shown. A, I, E and H represent the apical domain, intermediate domain, equatorial domain and the helical protrusion. T, D and Pi are ATP, ADP and phosphate ion. Reproduced from Nakagawa et al. (2014) © Elsevier.
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Further Reading

Bigotti MG and Clarke AR (2008) Chaperonins: the hunt for the Group II mechanism. Archives of Biochemistry and Biophysics 474 (2): 331–339.

Douglas NR, Reissmann S, Zhang J, et al. (2011) Dual action of ATP hydrolysis couples lid closure to substrate release into the group II chaperonin chamber. Cell 144 (2): 240–252.

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Macario AJ, Malz M and de Macario C (2004) Evolution of assisted protein folding: the distribution of the main chaperoning systems within the phylogenetic domain archaea. Frontiers in Bioscience 9: 1318–1332.

Nakagawa A, Moriya K, Arita M, et al. (2014) Dissection of the ATP‐dependent conformational change cycle of a group II chaperonin. Journal of Molecular Biology 426 (2): 447–459.

Sekiguchi H, Nakagawa A, Moriya K, et al. (2013) ATP dependent rotational motion of group II chaperonin observed by X‐ray single molecule tracking. PLoS One 8 (5): e64176.

Willison KR (2011) Structural changes underlying allostery in group II chaperonins. Structure 19 (6): 754–755.

Yamamoto YY, Abe Y, Moriya K, et al. (2014) Inter‐ring communication is dispensable in the reaction cycle of group II chaperonins. Journal of Molecular Biology 426 (14): 2667–2678.

Yébenes H, Mesa P, Muñoz IG, et al. (2011) Chaperonins: two rings for folding. Trends in Biochemical Sciences 36 (8): 424–432.

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Yamamoto, Yohei Y, and Yohda, Masafumi(Jan 2016) Thermosome: A Group II Chaperonin of Archaea. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0026332]