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The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core.

Abstract：

:Redox-regulated effector systems that counteract oxidative stress are essential for all forms of life. Here we uncover a new paradigm for sensing oxidative stress centred on the hydrophobic core of a sensor protein. RsrA is an archetypal zinc-binding anti-sigma factor that responds to disulfide stress in the cytoplasm of Actinobacteria. We show that RsrA utilizes its hydrophobic core to bind the sigma factor σ(R) preventing its association with RNA polymerase, and that zinc plays a central role in maintaining this high-affinity complex. Oxidation of RsrA is limited by the rate of zinc release, which weakens the RsrA-σ(R) complex by accelerating its dissociation. The subsequent trigger disulfide, formed between specific combinations of RsrA's three zinc-binding cysteines, precipitates structural collapse to a compact state where all σ(R)-binding residues are sequestered back into its hydrophobic core, releasing σ(R) to activate transcription of anti-oxidant genes.

journal_name

Nat Commun

journal_title

Nature communications

authors

Rajasekar KV,Zdanowski K,Yan J,Hopper JT,Francis ML,Seepersad C,Sharp C,Pecqueur L,Werner JM,Robinson CV,Mohammed S,Potts JR,Kleanthous C

doi

10.1038/ncomms12194

subject

Has Abstract

pub_date

2016-07-19 00:00:00

pages

12194

issn

2041-1723

pii

ncomms12194

journal_volume

7

pub_type

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