{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T00:34:57Z","timestamp":1791333297196,"version":"4.3.1"},"reference-count":36,"publisher":"National Academy of Sciences","issue":"18","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1999,8,31]]},"abstract":"<jats:p>\n                    <jats:italic>nifU<\/jats:italic>\n                    of nitrogen-fixing bacteria is involved in the synthesis of the Fe\u2013S cluster of nitrogenase. In a synthetic lethal screen with the mitochondrial heat shock protein (HSP)70,\n                    <jats:italic>SSQ1<\/jats:italic>\n                    , we identified a gene of\n                    <jats:italic>Saccharomyces cerevisiae<\/jats:italic>\n                    ,\n                    <jats:italic>NFU1<\/jats:italic>\n                    , which encodes a protein with sequence identity to the C-terminal domain of NifU. Two other yeast genes were found to encode proteins related to the N-terminal domain of bacterial NifU. They have been designated\n                    <jats:italic>ISU1<\/jats:italic>\n                    and\n                    <jats:italic>ISU2<\/jats:italic>\n                    . Isu1, Isu2, and Nfu1 are located in the mitochondrial matrix.\n                    <jats:italic>ISU<\/jats:italic>\n                    genes of yeast carry out an essential function, because a\n                    <jats:italic>\u0394isu1\u0394isu2<\/jats:italic>\n                    strain is inviable. Growth of\n                    <jats:italic>\u0394nfu1\u0394 isu1<\/jats:italic>\n                    cells is significantly compromised, allowing assessment of the physiological roles of Nfu and Isu proteins. Mitochondria from\n                    <jats:italic>\u0394nfu1\u0394isu1<\/jats:italic>\n                    cells have decreased activity of several respiratory enzymes that contain Fe\u2013S clusters. As a result,\n                    <jats:italic>\u0394nfu1\u0394isu1<\/jats:italic>\n                    cells grow poorly on carbon sources requiring respiration.\n                    <jats:italic>\u0394nfu1\u0394isu1<\/jats:italic>\n                    cells also accumulate abnormally high levels of iron in their mitochondria, similar to\n                    <jats:italic>\u0394ssq1<\/jats:italic>\n                    cells, indicating a role for these proteins in iron metabolism. We suggest that\n                    <jats:italic>NFU1<\/jats:italic>\n                    and\n                    <jats:italic>ISU1<\/jats:italic>\n                    gene products play a role in iron homeostasis, perhaps in assembly, insertion, and\/or repair of mitochondrial Fe\u2013S clusters. The conservation of these protein domains in many organisms suggests that this role has been conserved throughout evolution.\n                  <\/jats:p>","DOI":"10.1073\/pnas.96.18.10206","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:38:21Z","timestamp":1027679901000},"page":"10206-10211","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":263,"title":["Evidence for a conserved system for iron metabolism in the mitochondria of\n                    <i>Saccharomyces cerevisiae<\/i>"],"prefix":"10.1073","volume":"96","author":[{"given":"Brenda","family":"Schilke","sequence":"first","affiliation":[{"name":"Department of Biomolecular Chemistry and Institute for Enzyme Research and the Department of Biochemistry, University of Wisconsin, 1300 University Avenue, Madison, WI 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