{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,24]],"date-time":"2025-09-24T09:58:37Z","timestamp":1758707917734},"reference-count":60,"publisher":"Microbiology Society","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2006,9,1]]},"abstract":"<jats:p>Copper amine oxidases (CAOs) are found in almost every living kingdom. Although<jats:italic>Saccharomyces cerevisiae<\/jats:italic>is one of the few yeast species that lacks an endogenous CAO, heterologous gene expression of CAOs from other organisms produces a functional enzyme. To begin to characterize their function and mechanisms of copper acquisition, two putative<jats:italic>cao<\/jats:italic><jats:sup>+<\/jats:sup>genes from<jats:italic>Schizosaccharomyces pombe<\/jats:italic>were expressed in<jats:italic>S. cerevisiae<\/jats:italic>. Expression of<jats:italic>spao1<\/jats:italic><jats:sup>+<\/jats:sup>resulted in the production of an active enzyme capable of catalysing the oxidative deamination of primary amines. On the other hand, expression of<jats:italic>spao2<\/jats:italic><jats:sup>+<\/jats:sup>failed to produce an active CAO. Using a functional<jats:italic>spao1<\/jats:italic><jats:sup>+<\/jats:sup>\u2013<jats:italic>GFP<\/jats:italic>fusion allele, the SPAO1 protein was localized in the cytosol. Under copper-limiting conditions, yeast cells harbouring deletions of the<jats:italic>MAC1<\/jats:italic>,<jats:italic>CTR1<\/jats:italic>and<jats:italic>CTR3<\/jats:italic>genes were defective in amine oxidase activity. Likewise,<jats:italic>atx1<\/jats:italic>\u0394 null cells exhibited no CAO activity, while<jats:italic>ccc2<\/jats:italic>\u0394 mutant cells exhibited decreased levels of amine oxidase activity, and mutations in<jats:italic>cox17<\/jats:italic>\u0394 and<jats:italic>ccs1<\/jats:italic>\u0394 did not cause any defects in this activity. Copper-deprived<jats:italic>S. cerevisiae<\/jats:italic>cells expressing<jats:italic>spao1<\/jats:italic><jats:sup>+<\/jats:sup>required a functional<jats:italic>atx1<\/jats:italic><jats:sup>+<\/jats:sup>gene for growth on minimal medium containing ethylamine as the sole nitrogen source. Under these conditions, the inability of the<jats:italic>atx1<\/jats:italic>\u0394 cells to utilize ethylamine correlated with the lack of SPAO1 activity, in spite of the efficient expression of the protein. Cells carrying a disrupted<jats:italic>ccc2<\/jats:italic>\u0394 allele exhibited only weak growth on ethylamine medium containing a copper chelator. The results of these studies reveal that expression of the heterologous<jats:italic>spao1<\/jats:italic><jats:sup>+<\/jats:sup>gene in<jats:italic>S. cerevisiae<\/jats:italic>is required for its growth in medium containing ethylamine as the sole nitrogen source, and that expression of an active<jats:italic>Schiz. pombe<\/jats:italic>SPAO1 protein in<jats:italic>S. cerevisiae<\/jats:italic>depends on the acquisition of copper through the high-affinity copper transporters Ctr1 and Ctr3, and the copper chaperone Atx1.<\/jats:p>","DOI":"10.1099\/mic.0.28998-0","type":"journal-article","created":{"date-parts":[[2006,8,31]],"date-time":"2006-08-31T20:32:03Z","timestamp":1157056323000},"page":"2819-2830","source":"Crossref","is-referenced-by-count":17,"title":["Mechanisms of copper loading on the Schizosaccharomyces pombe copper amine oxidase 1 expressed in Saccharomyces cerevisiae"],"prefix":"10.1099","volume":"152","author":[{"given":"Julie","family":"Lalibert\u00e9","sequence":"first","affiliation":[{"name":"D\u00e9partement de Biochimie, Universit\u00e9 de Sherbrooke, 3001 12e Avenue Nord, Sherbrooke, Qu\u00e9bec J1H 5N4, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Simon","family":"Labb\u00e9","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Biochimie, Universit\u00e9 de Sherbrooke, 3001 12e Avenue Nord, Sherbrooke, Qu\u00e9bec J1H 5N4, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"53584","DOI":"10.1074\/jbc.M408099200","article-title":"Yeast Cox17 solution structure and copper(I) binding","volume":"279","author":"Abajian","year":"2004","journal-title":"J Biol Chem"},{"key":"R2","doi-asserted-by":"crossref","first-page":"8415","DOI":"10.1074\/jbc.M008389200","article-title":"Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states","volume":"276","author":"Banci","year":"2001","journal-title":"J Biol Chem"},{"key":"R3","doi-asserted-by":"crossref","first-page":"15472","DOI":"10.1074\/jbc.M011256200","article-title":"The fission yeast copper-sensing transcription factor Cuf1 regulates the copper transporter gene expression through an Ace1\/Amt1-like recognition sequence","volume":"276","author":"Beaudoin","year":"2001","journal-title":"J Biol Chem"},{"key":"R4","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1099\/mic.0.28392-0","article-title":"Functional dissection of Ctr4 and Ctr5 amino-terminal regions reveals motifs with redundant roles in copper transport","volume":"152","author":"Beaudoin","year":"2006","journal-title":"Microbiology"},{"key":"R5","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1002\/(SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2-2","article-title":"Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications","volume":"14","author":"Brachmann","year":"1998","journal-title":"Yeast"},{"key":"R6","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1016\/j.abb.2004.03.034","article-title":"Copper-containing amine oxidases. 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