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- W2159744669 abstract "Summary Genetic studies in the tuberculosis mouse model have suggested that mycobacterial metal efflux systems, such as the P 1B4 ‐ATPase CtpD, are important for pathogenesis. The specificity for substrate metals largely determines the function of these ATPases; however, various substrates have been reported for bacterial and plant P 1B4 ‐ATPases leaving their function uncertain. Here we describe the functional role of the CtpD protein of Mycobacterium smegmatis . An M. smegmatis mutant strain lacking the ctpD gene was hypersensitive to Co 2+ and Ni 2+ and accumulated these metals in the cytoplasm. ctpD transcription was induced by both Co 2+ and superoxide stress. Biochemical characterization of heterologously expressed, affinity‐purified CtpD showed that this ATPase is activated by Co 2+ , Ni 2+ and to a lesser extend Zn 2+ (20% of maximum activity). The protein was also able to bind one Co 2+ , Ni 2+ or Zn 2+ to its transmembrane transport site. These observations indicate that CtpD is important for Co 2+ and Ni 2+ homeostasis in M. smegmatis , and that M. tuberculosis CtpD orthologue could be involved in metal detoxification and resisting cellular oxidative stress by modulating the intracellular concentration of these metals." @default.
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- W2159744669 date "2012-05-17" @default.
- W2159744669 modified "2023-10-16" @default.
- W2159744669 title "Role in metal homeostasis of CtpD, a Co2+ transporting P1B4-ATPase of Mycobacterium smegmatis" @default.
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- W2159744669 doi "https://doi.org/10.1111/j.1365-2958.2012.08082.x" @default.
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