{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,12]],"date-time":"2026-10-12T22:54:44Z","timestamp":1791845684719,"version":"4.3.4"},"reference-count":49,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2017,10,18]],"date-time":"2017-10-18T00:00:00Z","timestamp":1508284800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2017,10,25]],"date-time":"2017-10-25T00:00:00Z","timestamp":1508889600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mSphere"],"published-print":{"date-parts":[[2017,10,25]]},"abstract":"<jats:p>\n            As mechanisms of copper toxicity are emerging, bacterial processing of intracellular copper, specifically inside\n            <jats:named-content content-type=\"genus-species\">Streptococcus pneumoniae<\/jats:named-content>\n            , 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\n            <jats:sup>2+<\/jats:sup>\n            to Cu\n            <jats:sup>1+<\/jats:sup>\n            . 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.\n          <\/jats:p>","DOI":"10.1128\/msphere.00372-17","type":"journal-article","created":{"date-parts":[[2017,10,19]],"date-time":"2017-10-19T00:25:36Z","timestamp":1508372736000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":30,"title":["Copper Chaperone CupA and Zinc Control CopY Regulation of the Pneumococcal\n            <i>cop<\/i>\n            Operon"],"prefix":"10.1128","volume":"2","author":[{"given":"Miranda J.","family":"Neubert","sequence":"first","affiliation":[{"name":"Department of Immunobiology, University of Arizona, Tucson, Arizona, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elizabeth A.","family":"Dahlmann","sequence":"additional","affiliation":[{"name":"Department of Immunobiology, University of Arizona, Tucson, Arizona, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew","family":"Ambrose","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Sciences, University of Arizona, Tucson, Arizona, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6347-0208","authenticated-orcid":false,"given":"Michael D. 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