{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,30]],"date-time":"2025-07-30T16:07:42Z","timestamp":1753891662795,"version":"3.41.2"},"reference-count":61,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2024,8,23]],"date-time":"2024-08-23T00:00:00Z","timestamp":1724371200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Microbiol."],"abstract":"<jats:sec><jats:title>Introduction<\/jats:title><jats:p>Translation is a fundamental process of life. In eukaryotes, the elongation step of translation is highly conserved and is driven by eukaryotic translation elongation factors (eEF)1A and eEF2. A significant variation of the elongation is the activity of eukaryotic elongation factor (eEF) 3 in <jats:italic>Saccharomyces cerevisiae<\/jats:italic> encoded by the gene yeast elongation factor (<jats:italic>YEF3<\/jats:italic>) with orthologs in all fungal species, a few algae, and some protists. In <jats:italic>S. cerevisiae, YEF3<\/jats:italic> is an essential gene and eEF3 plays a critical role in translation elongation, as it promotes binding of the ternary complex acylated-Transfer RNA (tRNA)\u2014eEF1A\u2014Guanosine-5'-triphosphate (GTP) to the aminoacyl (A) site of the ribosome, the release of uncharged tRNAs after peptide translocation, and ribosome recycling. Even though <jats:italic>YEF3<\/jats:italic> was discovered more than 40 years ago, eEF3 has been characterized almost exclusively in <jats:italic>S. cerevisiae<\/jats:italic>.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>We undertook an <jats:italic>in vivo<\/jats:italic> genetic approach to assess the functional conservation of <jats:italic>eEF3<\/jats:italic> across phylogenetically distant fungal species.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>We found that <jats:italic>eEF3<\/jats:italic> from <jats:italic>Zygosaccharomyces rouxii<\/jats:italic> and <jats:italic>Candida glabrata<\/jats:italic> (both belonging to <jats:italic>phylum<\/jats:italic> Ascomycota), <jats:italic>Ustilago maydis<\/jats:italic> (<jats:italic>phylum<\/jats:italic> Basidiomycota), and <jats:italic>Gonapodya prolifera<\/jats:italic> (<jats:italic>phylum<\/jats:italic> Monoblepharomycota), but not <jats:italic>Aspergillus nidulans<\/jats:italic> (<jats:italic>phylum<\/jats:italic> Ascomycota), supported the growth of <jats:italic>S. cerevisiae<\/jats:italic> lacking the endogenous <jats:italic>YEF3<\/jats:italic> gene. We also proved that <jats:italic>eEF3<\/jats:italic> is an essential gene in the ascomycetes <jats:italic>C. glabrata<\/jats:italic> and <jats:italic>A. nidulans<\/jats:italic>.<\/jats:p><\/jats:sec><jats:sec><jats:title>Discussion<\/jats:title><jats:p>Given that most existing knowledge on fungal translation has only been obtained from <jats:italic>S. cerevisiae<\/jats:italic>, our findings beyond this organism showed variability in the elongation process in Fungi. We also proved that <jats:italic>eEF3<\/jats:italic> is essential in pathogenic fungi, opening the possibility of using eEF3 as a target to fight candidiasis.<\/jats:p><\/jats:sec>","DOI":"10.3389\/fmicb.2024.1438900","type":"journal-article","created":{"date-parts":[[2024,8,23]],"date-time":"2024-08-23T16:37:55Z","timestamp":1724431075000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":1,"title":["The gene YEF3 function encoding translation elongation factor eEF3 is partially conserved across fungi"],"prefix":"10.3389","volume":"15","author":[{"given":"Giovanna","family":"Maldonado","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alejandra","family":"Garc\u00eda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Saturnino","family":"Herrero","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Irene","family":"Casta\u00f1o","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Altmann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reinhard","family":"Fischer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Greco","family":"Hern\u00e1ndez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1965","published-online":{"date-parts":[[2024,8,23]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"12145","DOI":"10.1016\/S0021-9258(18)63833-5","article-title":"A mammalian translation initiation factor can substitute for its yeast homologue in vivo","volume":"264","author":"Altmann","year":"1989","journal-title":"J. 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