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. 2013 May 25;4(6):432–444. doi: 10.1007/s13238-013-3026-9

Flexible interwoven termini determine the thermal stability of thermosomes

Kai Zhang 1,3, Li Wang 2, Yanxin Liu 4, Kwok-Yan Chan 4, Xiaoyun Pang 1, Klaus Schulten 4, Zhiyang Dong 2, Fei Sun 1,✉
PMCID: PMC3740188  NIHMSID: NIHMS496021  PMID: 23709365

Abstract

Group II chaperonins, which assemble as double-ring complexes, assist in the refolding of nascent peptides or denatured proteins in an ATP-dependent manner. The molecular mechanism of group II chaperonin assembly and thermal stability is yet to be elucidated. Here, we selected the group II chaperonins (cpn-α and cpn-β), also called thermosomes, from Acidianus tengchongensis and investigated their assembly and thermal stability. We found that the binding of ATP or its analogs contributed to the successful assembly of thermosomes and enhanced their thermal stabilities. Cpn-β is more thermally stable than cpn-α, while the thermal stability of the hetero thermosome cpn-αβ is intermediate. Cryo-electron microscopy reconstructions of cpn-α and cpn-β revealed the interwoven densities of their non-conserved flexible N/C-termini around the equatorial planes. The deletion or swapping of their termini and pH-dependent thermal stability assays revealed the key role of the termini electrostatic interactions in the assembly and thermal stability of the thermosomes.

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Keywords: group II chaperonin, thermosome, thermal stability, self-assembly, flexible terminus

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Electronic Supplementary Material

Supplementary material is available for this article at 10.1007/s13238-013-3026-9 and is accessible for authorized users.

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Supplementary Materials

13238_2013_3026_MOESM1_ESM.zip (5.7MB, zip)

Supplementary material, approximately 1.22 MB.

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Supplementary material, approximately 3.92 MB.

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Supplementary material, approximately 666 KB.

13238_2013_3026_MOESM4_ESM.pdf (76.3KB, pdf)

Supplementary material, approximately 76.2 KB.

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Supplementary material, approximately 1.22 MB.

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Supplementary material, approximately 1.22 MB.

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