Analysis of the interaction mode between hyperthermophilic archaeal group II chaperonin and prefoldin using a platform of chaperonin oligomers of various subunit arrangements

作者：Sahlan Muhamad; Kanzaki Taro; Zako Tamotsu; Maeda Mizuo; Yohda Masafumi^*

来源：Biochimica et Biophysica Acta-Proteins and Proteomics, 2010, 1804(9): 1810-1816.

DOI：10.1016/j.bbapap.2010.04.013

• Prefoldin
• Chaperonin
• Binding mode
• Molecular chaperone
• Surface plasmon resonance

Prefoldin is a co-chaperone that captures an unfolded protein substrate and transfers it to the group II chaperonin for completion of protein folding. Group II chaperonin of a hyperthermophilic archaeon, Thermococcus strain KS-1, interacts and cooperates with archaeal prefoldins. Although the interaction sites within chaperonin and prefoldin have been analyzed, the binding mode between jellyfish-like hexameric prefoldin and the double octameric ring group ll chaperonin remains unclear. As prefoldin binds the chaperonin beta subunit more strongly than the alpha subunit, we analyzed the binding mode between prefoldin and chaperonin in the context of Thermococcus group ll chaperonin complexes of various subunit compositions and arrangements. The oligomers exhibited various affinities for prefoldins according to the number and order of subunits. Binding affinity increased with the number of Cpn beta subunits. Interestingly, chaperonin complexes containing two beta subunits adjacently exhibited stronger affinities than other chaperonin complexes containing the same number of beta subunits. The result suggests that all four beta tentacles of prefoldin interact with the helical protrusions of CPN in the PFD CPN complex as the previously proposed model that two adjacent PFD 0 subunits seem to interact with two CPN adjacent subunits.

• 出版日期2010-9