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Structure and function of archaeal prefoldin, a co-chaperone of group II chaperonin
Akashi Ohtaki1,Keiichi Noguchi1,Masafumi Yohda1
1
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei, Tokyo 184-8588, Japan
DOI: 10.2741/3641 Volume 15 Issue 2, pp.708-717
Published: 01 January 2010
Abstract

Molecular chaperones are key cellular components involved in the maintenance of protein homeostasis and other unrelated functions. Prefoldin is a chaperone that acts as a co-factor of group II chaperonins in eukaryotes and archaea. It assists proper folding of protein by capturing nonnative proteins and delivering it to the group II chaperonin. Eukaryotic prefoldin is a multiple subunit complex composed of six different polypeptide chains. Archaeal prefoldin, on the other hand, is a heterohexameric complex composed of two alpha and four beta subunits, and forms a double beta barrel assembly with six long coiled coils protruding from it like a jellyfish with six tentacles. Based on the structural information of the archaeal prefoldin, substrate recognition and prefoldin-chaperonin binding mechanisms have been investigated. In this paper, we review a series of studies on the molecular mechanisms of archaeal PFD function. Particular emphasis will be placed on the molecular structures revealed by X-ray crystallography and molecular dynamics induced by binding to nonnative protein substrates.

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Akashi Ohtaki, Keiichi Noguchi, Masafumi Yohda. Structure and function of archaeal prefoldin, a co-chaperone of group II chaperonin. Frontiers in Bioscience-Landmark. 2010. 15(2); 708-717.