Molecular mechanism of protein folding by group II chaperonin and prefoldin of hyperthermophilic archaea

Masafumi Yohda; Ryo Iizuka; Tamotsu Zako; Takao Yoshida

doi:10.11490/isea.2005.0.92.0

International Symposium on Extremophiles and Their Applications 2005

DOI https://doi.org/10.11490/isea.2005.0.92.0

Conference information

Host: Japan Agency for Marine-Earth Science and Technology

Co-host: Toyo University, Japan Society for the Promotion of Science

Genetics and Protein Functions IV

Molecular mechanism of protein folding by group II chaperonin and prefoldin of hyperthermophilic archaea

*Masafumi Yohda, Ryo Iizuka, Tamotsu Zako, Takao Yoshida

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Keywords: chaperone, chaperonin, prefoldin, hyperthrmophile, folding, archaea

CONFERENCE PROCEEDINGS FREE ACCESS

Pages 92-95

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Abstract

Group II chaperonins and prefoldins take important roles in protein folding and maintenance in hyperthermophilic archaea since only four types of molecular chaperones are encoded on their genomes. In this paper, we will describe recent results of our studies on protein folding cycles of a group II chaperonin and cooperation mechanism between a prefoldin and a group II chaperonin from hyperthermophilic archaea.

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