Abstract
SigR (sigma(R)) is a sigma factor responsible for inducing the thioredoxin system in response to oxidative stress in the antibiotic-producing, Gram-positive bacterium Streptomyces coelicolor A3(2). Here we identify a redox-sensitive, sigma(R)-specific anti-sigma factor, RsrA, which binds sigma(R) and inhibits sigma(R)-directed transcription in vitro only under reducing conditions. Exposure to H(2)O(2) or to the thiol-specific oxidant diamide caused the dissociation of the sigma(R)-RsrA complex, thereby allowing sigma(R)-dependent transcription. This correlated with intramolecular disulfide bond formation in RsrA. Thioredoxin was able to reduce oxidized RsrA, suggesting that sigma(R), RsrA and the thioredoxin system comprise a novel feedback homeostasis loop that senses and responds to changes in the intracellular thiol-disulfide redox balance.
Original language | English |
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Pages (from-to) | 4292-8 |
Number of pages | 7 |
Journal | EMBO Journal |
Volume | 18 |
Issue number | 15 |
DOIs | |
Publication status | Published - 1999 |
Keywords
- Amino Acid Sequence
- Bacterial Proteins
- Disulfides
- Mass Spectrometry
- Molecular Sequence Data
- Oxidation-Reduction
- Sequence Homology, Amino Acid
- Sigma Factor
- Substrate Specificity
- Surface Plasmon Resonance
- Thioredoxins
- Transcription Factors
- Transcription, Genetic