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Title:
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Structural determinants of multimerization and dissociation in 2-Cys peroxiredoxin chaperone function.
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Authors:
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Troussicot L; Department of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden; Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, 405 30 Göteborg, Sweden.
Burmann BM; Department of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden; Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, 405 30 Göteborg, Sweden. Electronic address: .
Molin M; Department of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Göteborg, Sweden; Department of Biology and Biological Engineering, Chalmers University of Technology, 405 30 Göteborg, Sweden. Electronic address: .
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Source:
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Structure (London, England : 1993) [Structure] 2021 Jul 01; Vol. 29 (7), pp. 640-654. Date of Electronic Publication: 2021 May 03.
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Publication Type:
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Journal Article; Research Support, Non-U.S. Gov't; Review
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Language:
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English
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Imprint Name(s):
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Publication: 2000- : Cambridge, Mass. : Cell Press
Original Publication: London : Current Biology, c1993-
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MeSH Terms:
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Peroxiredoxins/*chemistry
Peroxiredoxins/*metabolism
Humans ; Models, Molecular ; Protein Conformation ; Protein Multimerization ; Structure-Activity Relationship
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Contributed Indexing:
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Keywords: 2-Cys peroxiredoxin; Hsp40; chaperone function; dissociation; holdase activity; oligomerization; small heat shock protein
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Substance Nomenclature:
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EC 1.11.1.15 (Peroxiredoxins)
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Entry Date(s):
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Date Created: 20210504 Date Completed: 20220111 Latest Revision: 20220111
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Update Code:
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20240104
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DOI:
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10.1016/j.str.2021.04.007
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PMID:
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33945778
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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.
Competing Interests: Declaration of interests The authors declare no competing interests.
(Copyright © 2021 The Authors. Published by Elsevier Ltd.. All rights reserved.)
