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Chaperone activation and client binding of a 2-cysteine peroxiredoxin.

Abstract：

:Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as peroxidases under non-stress conditions or as chaperones during stress. The mechanism by which 2-Cys-Prxs switch functions remains to be defined. Our work focuses on Leishmania infantum mitochondrial 2-Cys-Prx, whose reduced, decameric subpopulation adopts chaperone function during heat shock, an activity that facilitates the transition from insects to warm-blooded host environments. Here, we have solved the cryo-EM structure of mTXNPx in complex with a thermally unfolded client protein, and revealed that the flexible N-termini of mTXNPx form a well-resolved central belt that contacts and encapsulates the unstructured client protein in the center of the decamer ring. In vivo and in vitro cross-linking studies provide further support for these interactions, and demonstrate that mTXNPx decamers undergo temperature-dependent structural rearrangements specifically at the dimer-dimer interfaces. These structural changes appear crucial for exposing chaperone-client binding sites that are buried in the peroxidase-active protein.

journal_name

Nat Commun

journal_title

Nature communications

authors

Teixeira F,Tse E,Castro H,Makepeace KAT,Meinen BA,Borchers CH,Poole LB,Bardwell JC,Tomás AM,Southworth DR,Jakob U

doi

10.1038/s41467-019-08565-8

subject

Has Abstract

pub_date

2019-02-08 00:00:00

pages

659

issue

1

issn

2041-1723

pii

10.1038/s41467-019-08565-8

journal_volume

10

pub_type

杂志文章

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