{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,28]],"date-time":"2026-08-28T02:33:34Z","timestamp":1787884414095,"version":"build-2784847793"},"reference-count":57,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2014,7,23]],"date-time":"2014-07-23T00:00:00Z","timestamp":1406073600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Czech Grant Agency","award":["CZ278885"],"award-info":[{"award-number":["CZ278885"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2014,9]]},"abstract":"Summary<\/jats:title>\n \n Cytosolic and nuclear iron\u2010sulphur (\n Fe<\/jats:styled-content>\n \/\n S<\/jats:styled-content>\n ) proteins include essential components involved in protein translation,\n DNA<\/jats:styled-content>\n synthesis and\n DNA<\/jats:styled-content>\n repair. In yeast and human cells, assembly of their\n Fe<\/jats:styled-content>\n \/\n S<\/jats:styled-content>\n cofactor is accomplished by the\n CIA<\/jats:styled-content>\n (cytosolic iron\u2010sulphur protein assembly) machinery comprised of some 10 proteins. To investigate the extent of conservation of the\n CIA<\/jats:styled-content>\n pathway, we examined its importance in the early\u2010branching eukaryote\n \n T<\/jats:italic>\n <\/jats:styled-content>\n rypanosoma brucei<\/jats:italic>\n that encodes all known\n CIA<\/jats:styled-content>\n factors. Upon\n RNAi<\/jats:styled-content>\n \u2010mediated ablation of individual, early\u2010acting\n CIA<\/jats:styled-content>\n proteins, no major defects were observed in both procyclic and bloodstream stages. In contrast, parallel depletion of two\n CIA<\/jats:styled-content>\n components was lethal, and severely diminished cytosolic aconitase activity lending support for a direct role of the\n CIA<\/jats:styled-content>\n proteins in cytosolic\n Fe<\/jats:styled-content>\n \/\n S<\/jats:styled-content>\n protein biogenesis. In support of this conclusion, the\n \n T<\/jats:italic>\n <\/jats:styled-content>\n . brucei<\/jats:italic>\n \u2005\n CIA<\/jats:styled-content>\n proteins complemented the growth defects of their respective yeast\n CIA<\/jats:styled-content>\n depletion mutants. Finally, the\n \n T<\/jats:italic>\n <\/jats:styled-content>\n . brucei<\/jats:italic>\n \u2005\n CIA<\/jats:styled-content>\n factor\n T<\/jats:styled-content>\n ah18 was characterized as a flavoprotein, while its binding partner\n D<\/jats:styled-content>\n re2 functions as a\n Fe<\/jats:styled-content>\n \/\n S<\/jats:styled-content>\n protein. Together, our results demonstrate the essential and conserved function of the\n CIA<\/jats:styled-content>\n pathway in cytosolic\n Fe<\/jats:styled-content>\n \/\n S<\/jats:styled-content>\n protein assembly in both developmental stages of this representative of supergroup\n E<\/jats:styled-content>\n xcavata.\n <\/jats:p>","DOI":"10.1111\/mmi.12706","type":"journal-article","created":{"date-parts":[[2014,7,8]],"date-time":"2014-07-08T22:17:07Z","timestamp":1404857827000},"page":"897-910","source":"Crossref","is-referenced-by-count":26,"title":["Cytosolic iron\u2010sulphur protein assembly is functionally conserved and essential in procyclic and bloodstream\n \n T<\/i>\n <\/scp>\n rypanosoma brucei<\/i>"],"prefix":"10.1111","volume":"93","author":[{"given":"Somsuvro","family":"Basu","sequence":"first","affiliation":[{"name":"Biology Centre Institute of Parasitology 37005 \u010cesk\u00e9 Bud\u011bjovice (Budweis) Czech Republic"},{"name":"Faculty of Sciences University of South Bohemia 37005 \u010cesk\u00e9 Bud\u011bjovice (Budweis) Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daili J.","family":"Netz","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Zytobiologie und Zytopathologie Philipps\u2010Universit\u00e4t 35033 Marburg Germany"},{"name":"Max\u2010Planck\u2010Institut f\u00fcr terrestrische Mikrobiologie 35043 Marburg Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander C.","family":"Haindrich","sequence":"additional","affiliation":[{"name":"Faculty of Sciences University of South Bohemia 37005 \u010cesk\u00e9 Bud\u011bjovice (Budweis) Czech Republic"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nils","family":"Herlerth","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Zytobiologie und Zytopathologie Philipps\u2010Universit\u00e4t 35033 Marburg Germany"},{"name":"Max\u2010Planck\u2010Institut f\u00fcr terrestrische Mikrobiologie 35043 Marburg Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thibaut J.","family":"Lagny","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Zytobiologie und Zytopathologie Philipps\u2010Universit\u00e4t 35033 Marburg Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonio J.","family":"Pierik","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Zytobiologie und Zytopathologie Philipps\u2010Universit\u00e4t 35033 Marburg Germany"},{"name":"Faculty of Chemistry \u2013 Biochemistry University of Kaiserslautern 67663 Kaiserslautern Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roland","family":"Lill","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Zytobiologie und Zytopathologie Philipps\u2010Universit\u00e4t 35033 Marburg Germany"},{"name":"Max\u2010Planck\u2010Institut f\u00fcr terrestrische Mikrobiologie 35043 Marburg Germany"},{"name":"LOEWE Zentrum f\u00fcr Synthetische 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