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

Karthik V. Rajasekar, Konrad Zdanowski, Jun Yan, Jonathan T. S. Hopper, Marie-Louise R. Francis, Colin Seepersad, Connor Sharp, Ludovic Pecqueur, Jörn M. Werner, Carol V. Robinson, Shabaz Mohammed, Jennifer R. Potts and Colin Kleanthous ()
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Karthik V. Rajasekar: University of Oxford
Konrad Zdanowski: University of York
Jun Yan: Chemistry Research Laboratory, University of Oxford
Jonathan T. S. Hopper: Chemistry Research Laboratory, University of Oxford
Marie-Louise R. Francis: University of Oxford
Colin Seepersad: University of Oxford
Connor Sharp: University of Oxford
Ludovic Pecqueur: School of Biological Sciences, University of Southampton
Jörn M. Werner: School of Biological Sciences, University of Southampton
Carol V. Robinson: Chemistry Research Laboratory, University of Oxford
Shabaz Mohammed: University of Oxford
Jennifer R. Potts: University of York
Colin Kleanthous: University of Oxford

Nature Communications, 2016, vol. 7, issue 1, 1-14

Abstract: 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 σR 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–σR 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 σR-binding residues are sequestered back into its hydrophobic core, releasing σR to activate transcription of anti-oxidant genes.

Date: 2016
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DOI: 10.1038/ncomms12194

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