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- W2042512144 abstract "The host–pathogen interactions in Mycobacterium tuberculosis infection are significantly influenced by redox stimuli and alterations in the levels of secreted antigens. The extracytoplasmic function (ECF) σ factor σ K governs the transcription of the serodominant antigens MPT70 and MPT83. The cellular levels of σ K are regulated by the membrane-associated anti-σ K (RskA) that localizes σ K in an inactive complex. The crystal structure of M. tuberculosis σ K in complex with the cytosolic domain of RskA (RskA cyto ) revealed a disulfide bridge in the −35 promoter-interaction region of σ K . Biochemical experiments reveal that the redox potential of the disulfide-forming cysteines in σ K is consistent with its role as a sensor. The disulfide bond in σ K influences the stability of the σ K –RskA cyto complex but does not interfere with σ K –promoter DNA interactions. It is noted that these disulfide-forming cysteines are conserved across homologues, suggesting that this could be a general mechanism for redox-sensitive transcription regulation." @default.
- W2042512144 created "2016-06-24" @default.
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- W2042512144 date "2014-03-19" @default.
- W2042512144 modified "2023-09-23" @default.
- W2042512144 title "Structural basis for the redox sensitivity of the<i>Mycobacterium tuberculosis</i>SigK–RskA σ–anti-σ complex" @default.
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- W2042512144 doi "https://doi.org/10.1107/s1399004714000121" @default.
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