Contribution of the C-Terminal Region of a Group II Chaperonin to its Interaction with Prefoldin and Substrate Transfer

Tamotsu Zako, Muhamad Sahlan, Sayaka Fujii, Yohei Y. Yamamoto, Phan The Tai, Kotaro Sakai, Mizuo Maeda, Masafumi Yohda

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8 Citations (Scopus)


Prefoldin is a molecular chaperone that captures an unfolded protein substrate and transfers it to a group II chaperonin. Previous studies have shown that the interaction sites for prefoldin are located in the helical protrusions of group II chaperonins. However, it does not exclude the possibility of the existence of other interaction sites. In this study, we constructed C-terminal truncation mutants of a group II chaperonin and examined the effects of these mutations on the chaperone's function and interaction with prefoldin. Whereas the mutants with up to 6 aa truncation from the C-terminus retained more than 90% chaperone activities for protecting citrate synthase from thermal aggregation and refolding of green fluorescent protein and isopropylmalate dehydrogenase, the truncation mutants showed decreased affinities for prefoldin. Consequently, the truncation mutants showed reduced transfer efficiency of the denatured substrate protein from prefoldin and subsequent chaperonin-dependent refolding. The results clearly show that the C-terminal region of group II chaperonins contributes to their interactions with prefoldin, the transfer of the substrate protein from prefoldin and its refolding.

Original languageEnglish
Pages (from-to)2405-2417
Number of pages13
JournalJournal of Molecular Biology
Issue number11
Publication statusPublished - 5 Jun 2016


  • Chaperone
  • Chaperonin
  • Prefoldin
  • Protein folding
  • Protein interaction


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