title: Hyperthermophilic archaeal prefoldin shows refolding activity at low temperature.
abstract: Prefoldin is a molecular chaperone that captures a protein-folding intermediate and transfers it to a group II chaperonin for correct folding. Previous studies of archaeal prefoldins have shown that prefoldin only possesses holdase activity and is unable to fold unfolded proteins by itself. In this study, we have demonstrated for the first time that a prefoldin from hyperthermophilic archaeon, Pyrococcus horikoshii OT3 (PhPFD), exhibits refolding activity for denatured lysozyme at temperatures relatively lower than physiologically active temperatures. The interaction between PhPFD and denatured lysozyme was investigated by use of a surface plasmon resonance sensor at various temperatures. Although PhPFD showed strong affinity for denatured lysozyme at high temperature, it exhibited relatively weak interactions at lower temperature. The protein-folding seems to occur through binding and release from PhPFD by virtue of the weak affinity. Our results also imply that prefoldin might be able to contribute to the folding of some cellular proteins whose affinity with prefoldin is weak.
authors.affiliation: Bioengineering Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. zako@riken.jp
authors.forename: Tamotsu
authors.initials: T
authors.lastname: Zako
authors.forename: Shinya
authors.initials: S
authors.lastname: Banba
authors.forename: Muhamad
authors.initials: M
authors.lastname: Sahlan
authors.forename: Masafumi
authors.initials: M
authors.lastname: Sakono
authors.forename: Naofumi
authors.initials: N
authors.lastname: Terada
authors.forename: Masafumi
authors.initials: M
authors.lastname: Yohda
authors.forename: Mizuo
authors.initials: M
authors.lastname: Maeda
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry*; D003080:Cold Temperature; D046529:Microscopy, Electron, Transmission; D018832:Molecular Chaperones / Q000737:chemistry*; D009113:Muramidase / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D043902:Pyrococcus horikoshii / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D018832:Molecular Chaperones; C112806:prefoldin; D009113:Muramidase