Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function
Reviewartikel, 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

Författare

Laura Troussicot

Wallenberg Lab.

Göteborgs universitet

Björn M. Burmann

Wallenberg Lab.

Göteborgs universitet

Mikael Molin

Chalmers, Biologi och bioteknik, Systembiologi

Göteborgs universitet

Structure

0969-2126 (ISSN)

Vol. 29 7 640-654

Ämneskategorier

Biofysik

Strukturbiologi

Teoretisk kemi

DOI

10.1016/j.str.2021.04.007

PubMed

33945778

Mer information

Senast uppdaterat

2021-07-05