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. 2008 Dec 5;191(5):1587–1594. doi: 10.1128/JB.01205-08

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FIG. 1. — MfpA_Mt inhibits the catalytic activity of M. tuberculosis DNA gyrase in topoisomerase assays. (A) Concentration-dependent inhibitory effect of MfpA_Mt on supercoiling activity of M. tuberculosis DNA gyrase. Supercoiling assays were performed using relaxed pBR322 as the substrate (TR) and final concentrations of MfpA_Mt (μM) as indicated. R, relaxed pBR322; S, supercoiled pBR322. (B) Concentration-dependent inhibitory effect of MfpA_Mt on ATP-independent relaxation of supercoiled DNA. Supercoiled pBR322 (TS) was the substrate. (C) Concentration-dependent inhibitory effect of MfpA_Mt on decatenation activity of M. tuberculosis DNA gyrase. Interlinked kDNA (kDNA) was used as the substrate (TI). Decatenated minicircles were visualized in three forms: relaxed (R), linearized (L), and supercoiled (S).