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- W2766440777 abstract "As mechanisms of copper toxicity are emerging, bacterial processing of intracellular copper, specifically inside Streptococcus pneumoniae , remains unclear. In this study, we investigated two proteins encoded by the copper export operon: the repressor, CopY, and the copper chaperone, CupA. Zinc suppressed transcription of the copper export operon by increasing the affinity of CopY for DNA. Furthermore, CupA was able to chelate copper from CopY not bound to DNA and reduce it from Cu 2+ to Cu 1+ . This reduced copper state is essential for bacterial copper export via CopA. In view of the fact that innate immune cells use copper to kill pathogenic bacteria, understanding the mechanisms of copper export could expose new small-molecule therapeutic targets that could work synergistically with copper against pathogenic bacteria." @default.
- W2766440777 created "2017-11-10" @default.
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- W2766440777 date "2017-10-25" @default.
- W2766440777 modified "2023-09-24" @default.
- W2766440777 title "Copper Chaperone CupA and Zinc Control CopY Regulation of the Pneumococcal <i>cop</i> Operon" @default.
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- W2766440777 doi "https://doi.org/10.1128/msphere.00372-17" @default.
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