{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T06:55:03Z","timestamp":1790837703274,"version":"4.1.0"},"reference-count":54,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2002,12,1]],"date-time":"2002-12-01T00:00:00Z","timestamp":1038700800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2002,12,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>In the unicellular green algae Chlamydomonas reinhardtii, high-affinity uptake of iron (Fe) requires an Fe3+-chelate reductase and an Fe transporter. Neither of these proteins nor their corresponding genes have been isolated. We previously identified, by analysis of differentially expressed plasma membrane proteins, an approximately 150-kD protein whose synthesis was induced under conditions of Fe-deficient growth. Based on homology of internal peptide sequences to the multicopper oxidase hephaestin, this protein was proposed to be a ferroxidase. A nucleotide sequence to the full-length cDNA clone for this ferroxidase-like protein has been obtained. Analysis of the primary amino acid sequence revealed a putative transmembrane domain near the amino terminus of the protein and signature sequences for two multicopper oxidase I motifs and one multicopper oxidase II motif. The ferroxidase-like gene was transcribed under conditions of Fe deficiency. Consistent with the role of a copper (Cu)-containing protein in Fe homeostasis, growth of cells in Cu-depleted media eliminated high-affinity Fe uptake, and Cu-deficient cells that were grown in optimal Fe showed greatly reduced Fe accumulation compared with control, Cu-sufficient cells. Reapplication of Cu resulted in the recovery of Fe transport activity. Together, these results were consistent with the participation of a ferroxidase in high-affinity Fe uptake in C. reinhardtii.<\/jats:p>","DOI":"10.1104\/pp.013060","type":"journal-article","created":{"date-parts":[[2002,12,12]],"date-time":"2002-12-12T18:22:30Z","timestamp":1039717350000},"page":"2039-2048","source":"Crossref","is-referenced-by-count":94,"title":["The Involvement of a Multicopper Oxidase in Iron Uptake by the Green Algae <i>Chlamydomonas reinhardtii<\/i>\n\u00a0"],"prefix":"10.1093","volume":"130","author":[{"given":"Alexandra","family":"Herbik","sequence":"first","affiliation":[{"name":"Applied Botany, Humboldt University Berlin, Invalidenstrasse 42, 10115 Berlin, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Bo\u0308lling","sequence":"additional","affiliation":[{"name":"Applied Botany, Humboldt University Berlin, Invalidenstrasse 42, 10115 Berlin, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas J.","family":"Buckhout","sequence":"additional","affiliation":[{"name":"Applied Botany, Humboldt University Berlin, Invalidenstrasse 42, 10115 Berlin, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2002,12,1]]},"reference":[{"key":"2021062513464807700_R1","doi-asserted-by":"crossref","first-page":"19906","DOI":"10.1074\/jbc.M000713200","article-title":"A novel mammalian iron-regulated protein involved in intracellular iron metabolism.","volume":"275","author":"Abboud","year":"2000","journal-title":"J Biol Chem"},{"key":"2021062513464807700_R2","doi-asserted-by":"crossref","first-page":"940","DOI":"10.1016\/S1357-2725(01)00063-2","article-title":"Chemistry and biology of eukaryotic iron metabolism.","volume":"33","author":"Aisen","year":"2001","journal-title":"Int J Biochem Cell Biol"},{"key":"2021062513464807700_R3","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1111\/j.1365-2958.1996.tb02485.x","article-title":"Molecular biology of iron acquisition in Saccharomyces cerevisiae.","volume":"20","author":"Askwith","year":"1996","journal-title":"Mol Microbiol"},{"key":"2021062513464807700_R4","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/0092-8674(94)90346-8","article-title":"The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.","volume":"76","author":"Askwith","year":"1994","journal-title":"Cell"},{"key":"2021062513464807700_R5","doi-asserted-by":"crossref","first-page":"22415","DOI":"10.1074\/jbc.273.35.22415","article-title":"Site-directed mutagenesis of the yeast multicopper oxidase Fet3p.","volume":"273","author":"Askwith","year":"1998","journal-title":"J Biol Chem"},{"key":"2021062513464807700_R6","doi-asserted-by":"crossref","first-page":"1116","DOI":"10.1074\/jbc.274.2.1116","article-title":"Ceruloplasmin ferroxidase activity stimulates cellular iron uptake by a trivalent cation-specific transport mechanism.","volume":"274","author":"Attieh","year":"1999","journal-title":"J Biol Chem"},{"key":"2021062513464807700_R7","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/0162-0134(84)85008-4","article-title":"Inhibition of ceruloplasmin and other copper oxidases by thiomolybdate.","volume":"22","author":"Chidambaram","year":"1984","journal-title":"J Inorg Biochem"},{"key":"2021062513464807700_R8","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/0003-2697(87)90021-2","article-title":"Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction.","volume":"162","author":"Chomczynski","year":"1987","journal-title":"Anal Biochem"},{"key":"2021062513464807700_R9","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1042\/bj3470749","article-title":"Involvement of NRAMP1 from Arabidopsis thaliana in iron transport.","volume":"347","author":"Curie","year":"2000","journal-title":"Biochem J"},{"key":"2021062513464807700_R10","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1038\/35053080","article-title":"Maize yellow stripe1 encodes a membrane protein directly involved in Fe(III) uptake.","volume":"409","author":"Curie","year":"2001","journal-title":"Nature"},{"key":"2021062513464807700_R11","doi-asserted-by":"crossref","first-page":"3869","DOI":"10.1073\/pnas.89.9.3869","article-title":"Ferric reductase of Saccharomyces cerevisiae: molecular characterization, role in iron uptake, and transcriptional control by iron.","volume":"89","author":"Dancis","year":"1992","journal-title":"Proc Natl Acad Sci USA"},{"key":"2021062513464807700_R12","doi-asserted-by":"crossref","first-page":"25660","DOI":"10.1016\/S0021-9258(18)47300-0","article-title":"The Saccharomyces cerevisiae copper transport protein (CTR1p). 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