期刊
Nature Communications
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12194
关键词
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资金
- BBSRC grant [BB/I008691/1]
- British Heart Foundation [FS/12/36/29588]
- Wellcome Trust [090658/Z/09/Z]
- MRC [U117533887]
- Biotechnology and Biological Sciences Research Council [BB/I008691/1, BB/I008691/2] Funding Source: researchfish
- British Heart Foundation [FS/12/36/29588] Funding Source: researchfish
- BBSRC [BB/I008691/1, BB/I008691/2] Funding Source: UKRI
- Wellcome Trust [090658/Z/09/Z] Funding Source: Wellcome Trust
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 sR 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-sigma(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 sR-binding residues are sequestered back into its hydrophobic core, releasing sR to activate transcription of anti-oxidant genes.
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