2013/05/24 by Kai Zhang, Li Wang, Yanxin Liu +5 · 2 citations
Biochemistry, Genetics and Molecular Biology · Materials Science · #Heat shock proteins research #Protein Structure and Dynamics #Enzyme Structure and Function
paper · doi:10.1007/s13238-013-3026-9
openalex publication_date 2013/05/24 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/22
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.