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

Counteracting oxidative stress is essential in all organisms. Here, the authors outline a mechanism used by actinomycete bacteria in which oxidation of zinc-binding RsrA blocks its interaction with σR by sequestering hydrophobic residues used to bind σRwithin its own core.

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Autores principales: 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, Colin Kleanthous
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Lenguaje:EN
Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/c89d901e44ac441eb22442e5e5cd39b3
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spelling oai:doaj.org-article:c89d901e44ac441eb22442e5e5cd39b32021-12-02T14:40:13ZThe anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core10.1038/ncomms121942041-1723https://doaj.org/article/c89d901e44ac441eb22442e5e5cd39b32016-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms12194https://doaj.org/toc/2041-1723Counteracting oxidative stress is essential in all organisms. Here, the authors outline a mechanism used by actinomycete bacteria in which oxidation of zinc-binding RsrA blocks its interaction with σR by sequestering hydrophobic residues used to bind σRwithin its own core.Karthik V. RajasekarKonrad ZdanowskiJun YanJonathan T. S. HopperMarie-Louise R. FrancisColin SeepersadConnor SharpLudovic PecqueurJörn M. WernerCarol V. RobinsonShabaz MohammedJennifer R. PottsColin KleanthousNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-14 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Colin Kleanthous
The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core
description Counteracting oxidative stress is essential in all organisms. Here, the authors outline a mechanism used by actinomycete bacteria in which oxidation of zinc-binding RsrA blocks its interaction with σR by sequestering hydrophobic residues used to bind σRwithin its own core.
format article
author 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
Colin Kleanthous
author_facet 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
Colin Kleanthous
author_sort Karthik V. Rajasekar
title The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core
title_short The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core
title_full The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core
title_fullStr The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core
title_full_unstemmed The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core
title_sort anti-sigma factor rsra responds to oxidative stress by reburying its hydrophobic core
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/c89d901e44ac441eb22442e5e5cd39b3
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