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In cyanobacteria Atx1 contributes towards the supply of copper to plastocyanin inside thylakoids but it is shown here that in copper-replete medium, copper can reach plastocyanin without Atx1. Unlike metallochaperone-independent copper-supply to superoxide dismutase in eukaryotes, glutathione is not essential for Atx1-independent supply to plastocyanin: Double mutants missing\n                    <jats:italic>atx1<\/jats:italic>\n                    and\n                    <jats:italic>gshB<\/jats:italic>\n                    (encoding glutathione synthetase) accumulate the same number of atoms of copper per cell in the plastocyanin pool as wild type. Critically, \u0394\n                    <jats:italic>atx1<\/jats:italic>\n                    \u0394\n                    <jats:italic>gshB<\/jats:italic>\n                    are hypersensitive to elevated copper relative to wild type cells and also relative to \u0394\n                    <jats:italic>gshB<\/jats:italic>\n                    single mutants with evidence that hypersensitivity arises due to the mislocation of copper to sites for other metals including iron and zinc. The zinc site on the amino-terminal domain (ZiaA\n                    <jats:sub>\n                      <jats:italic>N<\/jats:italic>\n                    <\/jats:sub>\n                    ) of the\n                    <jats:italic>P<\/jats:italic>\n                    <jats:sub>1<\/jats:sub>\n                    -type zinc-transporting ATPase is especially similar to the copper site of the Atx1 target PacS\n                    <jats:sub>\n                      <jats:italic>N<\/jats:italic>\n                    <\/jats:sub>\n                    , and ZiaA\n                    <jats:sub>\n                      <jats:italic>N<\/jats:italic>\n                    <\/jats:sub>\n                    will bind Cu(I) more tightly than zinc. An NMR model of a substituted-ZiaA\n                    <jats:sub>\n                      <jats:italic>N<\/jats:italic>\n                    <\/jats:sub>\n                    -Cu(I)-Atx1 heterodimer has been generated making it possible to visualize a juxtaposition of residues surrounding the ZiaA\n                    <jats:sub>\n                      <jats:italic>N<\/jats:italic>\n                    <\/jats:sub>\n                    zinc site, including Asp\n                    <jats:sub>18<\/jats:sub>\n                    , which normally repulse Atx1. Equivalent repulsion between bacterial copper metallochaperones and the amino-terminal regions of\n                    <jats:italic>P<\/jats:italic>\n                    <jats:sub>1<\/jats:sub>\n                    -type ATPases for metals other than Cu(I) is conserved, again consistent with a role for copper metallochaperones to withhold copper from binding sites for other metals.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1117515109","type":"journal-article","created":{"date-parts":[[2011,12,23]],"date-time":"2011-12-23T01:22:44Z","timestamp":1324603364000},"page":"95-100","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":90,"title":["Cyanobacterial metallochaperone inhibits deleterious side reactions of copper"],"prefix":"10.1073","volume":"109","author":[{"given":"Steve","family":"Tottey","sequence":"first","affiliation":[{"name":"Fraunhofer USA Center for Molecular Biotechnology, Newark, DE 19711"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carl J.","family":"Patterson","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Biophysical Sciences Institute, School of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucia","family":"Banci","sequence":"additional","affiliation":[{"name":"CERM (Centro di Ricerca di Risonanze Magnetiche) and Department of Chemistry, University of Florence, 50019 Sesto Fiorentino (FI), Italy;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ivano","family":"Bertini","sequence":"additional","affiliation":[{"name":"CERM (Centro di Ricerca di Risonanze Magnetiche) and Department of Chemistry, University of Florence, 50019 Sesto Fiorentino (FI), Italy;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabella C.","family":"Felli","sequence":"additional","affiliation":[{"name":"CERM (Centro di Ricerca di Risonanze Magnetiche) and Department of Chemistry, University of Florence, 50019 Sesto Fiorentino (FI), Italy;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Pavelkova","sequence":"additional","affiliation":[{"name":"CERM (Centro di Ricerca di Risonanze Magnetiche) and Department of Chemistry, University of Florence, 50019 Sesto Fiorentino (FI), Italy;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Samantha J.","family":"Dainty","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Biophysical Sciences Institute, School of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rafael","family":"Pernil","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Biophysical Sciences Institute, School of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kevin J.","family":"Waldron","sequence":"additional","affiliation":[{"name":"Cell and Molecular Biosciences, Medical School, University of Newcastle, Newcastle upon Tyne NE2 4HH, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew W.","family":"Foster","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Biophysical Sciences Institute, School of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, United Kingdom;"},{"name":"Cell and Molecular Biosciences, Medical School, University of Newcastle, Newcastle upon Tyne NE2 4HH, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nigel J.","family":"Robinson","sequence":"additional","affiliation":[{"name":"Department of Chemistry, Biophysical Sciences Institute, School of Biological and Biomedical Sciences, University of Durham, Durham DH1 3LE, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2011,12,22]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1126\/science.278.5339.817","article-title":"Delivering copper inside yeast and human cells","volume":"278","author":"Valentine JS","year":"1997","unstructured":"JS Valentine, EB Gralla, Delivering copper inside yeast and human cells. 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Proc Natl Acad Sci USA 96, 13363\u201313368 (1999).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1126\/science.278.5339.853","article-title":"Metal ion chaperone function of the soluble Cu(I) receptor Atx1","volume":"278","author":"Pufahl RA","year":"1997","unstructured":"RA Pufahl, et al., Metal ion chaperone function of the soluble Cu(I) receptor Atx1. Science 278, 853\u2013856 (1997).","journal-title":"Science"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"35334","DOI":"10.1074\/jbc.M404747200","article-title":"Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase","volume":"279","author":"Horng YC","year":"2004","unstructured":"YC Horng, PA Cobine, AB Maxfield, HS Carr, DR Winge, Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase. 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