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PMID: 23709365 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Flexible interwoven termini determine the thermal stability of thermosomes.

Protein & cell ·Vol. 4 ·No. 6 ·2013-06-00 ·Pages 432-44

Zhang K, Wang L, Liu Y, Chan KY, Pang X, Schulten K, Dong Z, Sun F

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.

MeSH Terms
Acidianus/metabolism Adenosine Triphosphate/metabolism Amino Acid Sequence Cryoelectron Microscopy Hydrogen-Ion Concentration Molecular Sequence Data Mutation Nucleotides/metabolism Protein Binding Protein Folding Protein Stability Protein Structure, Quaternary Sequence Alignment Static Electricity Temperature Thermosomes/chemistry,genetics,metabolism
Chemicals
Nucleotides Adenosine Triphosphate Thermosomes
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Zhang Kai
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
Wang Li
Liu Yanxin
Chan Kwok-Yan
Pang Xiaoyun
Schulten Klaus
Dong Zhiyang
Sun Fei
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Article Info
Journal
Protein & cell
Abbr.
Protein Cell
ISSN
1674-8018
Published
2013-06-00
Epub
2013-00-25
Pages
432-44
Language
English
Region
Germany
NLM ID
101532368
PMCID
PMC3740188
Subset
IM
Grants
NIGMS NIH HHS · P41 GM104601 · United States
NIGMS NIH HHS · 9P41GM104601 · United States
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