Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function
Review article, 2021

Peroxiredoxins (PRDXs) are abundant peroxidases present in all kingdoms of life. Recently, they have been shown to also carry out additional roles as molecular chaperones. To address this emerging supplementary function, this review focuses on structural studies of 2-Cys PRDX systems exhibiting chaperone activity. We provide a detailed understanding of the current knowledge of structural determinants underlying the chaperone function of PRDXs. Specifically, we describe the mechanisms which may modulate their quaternary structure to facilitate interactions with client proteins and how they are coordinated with the functions of other molecular chaperones. Following an overview of PRDX molecular architecture, we outline structural details of the presently best-characterized peroxiredoxins exhibiting chaperone function and highlight common denominators. Finally, we discuss the remarkable structural similarities between 2-Cys PRDXs, small HSPs, and J-domain-independent Hsp40 holdases in terms of their functions and dynamic equilibria between low- and high-molecular-weight oligomers.

small heat shock protein

holdase activity

Hsp40

dissociation

chaperone function

oligomerization

2-Cys peroxiredoxin

Author

Laura Troussicot

Wallenberg Lab.

University of Gothenburg

Björn M. Burmann

Wallenberg Lab.

University of Gothenburg

Mikael Molin

Chalmers, Biology and Biological Engineering, Systems and Synthetic Biology

University of Gothenburg

Structure

0969-2126 (ISSN)

Vol. 29 7 640-654

Subject Categories

Biophysics

Structural Biology

Theoretical Chemistry

DOI

10.1016/j.str.2021.04.007

PubMed

33945778

More information

Latest update

7/5/2021 1