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• W2066884843 abstract "σR is a sigma factor for transcribing genes to defend cells against oxidative stresses in the antibiotic-producing bacterium Streptomyces coelicolor. The availability of σR is regulated by RsrA, an anti-sigma factor, whose σR-binding activity is regulated by redox changes in the environment, via thiol–disulfide exchange. We found that reduced RsrA contains zinc in a stoichiometric amount, whereas oxidized form has very little: 1 mol of zinc per mol of RsrA was released upon oxidation as monitored by a chromogenic Zn-chelator, 4-(2-pyridylazo)-resorcinol (PAR). Measurement of zinc bound in several RsrA mutants of various cysteine and histidine substitutions suggested that C3, H7, C41, and C44 serve as zinc-binding sites. The zinc-binding and σR-binding activities of mutant proteins did not coincide, suggesting that zinc might not be absolutely required for the anti-sigma activity of RsrA. Zn-free apo-RsrA bound σR and inhibited σR-dependent transcription in vitro. Compared with Zn-RsrA, the anti-transcription activity of apo-RsrA was about threefold lower and its σR-binding affinity decreased by about ninefold when measured by surface plasmon resonance analysis. Apo-RsrA was more sensitive to protease, suggesting that zinc allows RsrA to maintain a more compact structure, optimized for binding σR. The cysteine pairs that form disulfide bonds were determined by MALDI-TOF mass spectrometry, revealing formation of the critical disulfide bond between C11 and one of the essential cysteine residues C41 or 44, most likely C44. An improved model for the mechanism of redox-modulation of RsrA was presented." @default.
• W2066884843 created "2016-06-24" @default.
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• W2066884843 date "2004-01-01" @default.
• W2066884843 modified "2023-09-25" @default.
• W2066884843 title "Redox-dependent Changes in RsrA, an Anti-sigma Factor in Streptomyces coelicolor: Zinc Release and Disulfide Bond Formation" @default.
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• W2066884843 doi "https://doi.org/10.1016/j.jmb.2003.10.065" @default.
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