{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T04:42:54Z","timestamp":1791434574659,"version":"4.3.3"},"reference-count":56,"publisher":"American Society for Microbiology","issue":"3","license":[{"start":{"date-parts":[[2004,6,1]],"date-time":"2004-06-01T00:00:00Z","timestamp":1086048000000},"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":["Eukaryot Cell"],"published-print":{"date-parts":[[2004,6]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The\n            <jats:italic>Cryptococcus neoformans LYS9<\/jats:italic>\n            gene (encoding saccharopine dehydrogenase) was cloned and found to be part of an evolutionarily conserved chimera with\n            <jats:italic>SPE3<\/jats:italic>\n            (encoding spermidine synthase).\n            <jats:italic>spe3-lys9<\/jats:italic>\n            ,\n            <jats:italic>spe3-LYS9<\/jats:italic>\n            , and\n            <jats:italic>SPE3-lys9<\/jats:italic>\n            mutants were constructed, and these were auxotrophic for lysine and spermidine, spermidine, and lysine, respectively. Thus,\n            <jats:italic>SPE3-LYS9<\/jats:italic>\n            encodes functional spermidine synthase and saccharopine dehydrogenase gene products. In contrast to\n            <jats:italic>Saccharomyces cerevisiae spe3<\/jats:italic>\n            mutants, the polyamine auxotrophy of\n            <jats:italic>C. neoformans spe3-LYS9<\/jats:italic>\n            mutants was not satisfied by spermine. In vitro phenotypes of\n            <jats:italic>spe3-LYS9<\/jats:italic>\n            mutants included reduced capsule and melanin production and growth rate, while\n            <jats:italic>SPE3-lys9<\/jats:italic>\n            mutants grew slowly at 30\u00b0C, were temperature sensitive in rich medium, and died upon lysine starvation. Consistent with the importance of saccharopine dehydrogenase and spermidine synthase in vitro,\n            <jats:italic>spe3-lys9<\/jats:italic>\n            mutants were avirulent and unable to survive in vivo and both functions individually contributed to virulence.\n            <jats:italic>SPE3-LYS9<\/jats:italic>\n            mRNA levels showed little evidence of being influenced by exogenous spermidine or lysine or starvation for spermidine or lysine; thus, any regulation is likely to be posttranscriptional. Expression in\n            <jats:italic>S. cerevisiae<\/jats:italic>\n            of the full-length\n            <jats:italic>C. neoformans SPE3-LYS9<\/jats:italic>\n            cDNA complemented a\n            <jats:italic>lys9<\/jats:italic>\n            mutant but not a\n            <jats:italic>spe3<\/jats:italic>\n            mutant. However, expression in\n            <jats:italic>S. cerevisiae<\/jats:italic>\n            of a truncated gene product, consisting of only\n            <jats:italic>C. neoformans SPE3<\/jats:italic>\n            , complemented a\n            <jats:italic>spe3<\/jats:italic>\n            mutant, suggesting possible modes of regulation. Therefore, we identified and describe a novel chimeric\n            <jats:italic>SPE3-LYS9<\/jats:italic>\n            gene, which may link spermidine and lysine biosynthesis in\n            <jats:italic>C. neoformans<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/ec.3.3.752-763.2004","type":"journal-article","created":{"date-parts":[[2004,6,9]],"date-time":"2004-06-09T17:22:25Z","timestamp":1086801745000},"page":"752-763","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":44,"title":["Novel Chimeric Spermidine Synthase-Saccharopine Dehydrogenase Gene (\n            <i>SPE3-LYS9<\/i>\n            ) in the Human Pathogen\n            <i>Cryptococcus neoformans<\/i>"],"prefix":"10.1128","volume":"3","author":[{"given":"Joanne M.","family":"Kingsbury","sequence":"first","affiliation":[{"name":"Department of Molecular Genetics and Microbiology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhonghui","family":"Yang","sequence":"additional","affiliation":[{"name":"Department of Molecular Genetics and Microbiology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tonya M.","family":"Ganous","sequence":"additional","affiliation":[{"name":"Department of Molecular Genetics and Microbiology"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gary M.","family":"Cox","sequence":"additional","affiliation":[{"name":"Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John H.","family":"McCusker","sequence":"additional","affiliation":[{"name":"Department of Molecular Genetics and Microbiology"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.178.9.2721-2724.1996"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1093\/jb\/117.2.339"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.159.1.429-432.1984"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/jcm.31.10.2819-2823.1993"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.94.5.1475-1479.1967"},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","unstructured":"Casadevall A. and J. 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