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

Muhamad Sahlan, Taro Kanzaki, Tamotsu Zako, Mizuo Maeda, Masafumi Yohda

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

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 β subunit more strongly than the α 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 Cpnβ subunits. Interestingly, chaperonin complexes containing two β subunits adjacently exhibited stronger affinities than other chaperonin complexes containing the same number of β subunits. The result suggests that all four β tentacles of prefoldin interact with the helical protrusions of CPN in the PFD-CPN complex as the previously proposed model that two adjacent PFD β subunits seem to interact with two CPN adjacent subunits.

Original languageEnglish
Pages (from-to)1810-1816
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1804
Issue number9
DOIs
Publication statusPublished - Sep 2010

Keywords

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

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