title: Analysis of the interaction mode between hyperthermophilic archaeal group II chaperonin and prefoldin using a platform of chaperonin oligomers of various subunit arrangements.
abstract: 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 II 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 II 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 Cpnbeta 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 beta subunits seem to interact with two CPN adjacent subunits.
authors.affiliation: Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei-shi, Tokyo 184-8588, Japan.
authors.forename: Muhamad
authors.initials: M
authors.lastname: Sahlan
authors.forename: Taro
authors.initials: T
authors.lastname: Kanzaki
authors.forename: Tamotsu
authors.initials: T
authors.lastname: Zako
authors.forename: Mizuo
authors.initials: M
authors.lastname: Maeda
authors.forename: Masafumi
authors.initials: M
authors.lastname: Yohda
mesh_terms: D001105:Archaea / Q000378:metabolism*; D019843:Archaeal Proteins / Q000378:metabolism*; D018833:Chaperonins; D056385:Group II Chaperonins / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding; D055503:Protein Multimerization; D021122:Protein Subunits; D020349:Surface Plasmon Resonance
chemical_list: D019843:Archaeal Proteins; D018832:Molecular Chaperones; D021122:Protein Subunits; C112806:prefoldin; D018833:Chaperonins; D056385:Group II Chaperonins