Hyperthermophilic archaeal prefoldin shows refolding activity at low temperature

Tamotsu Zako, Shinya Banba, Muhamad Sahlan, Masafumi Sakono, Naofumi Terada, Masafumi Yohda, Mizuo Maeda

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)467-470
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 1 Jan 2010


  • Interaction study
  • Lysozyme
  • Molecular chaperone
  • Prefoldin
  • Refolding activity
  • Surface plasmon resonance


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