{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,28]],"date-time":"2025-10-28T00:28:08Z","timestamp":1761611288813},"reference-count":44,"publisher":"Proceedings of the National Academy of Sciences","issue":"34","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2011,8,23]]},"abstract":"<jats:p>\n            In a restricted group of opportunistic fungal pathogens the universal leucine CUG codon is translated both as serine (97%) and leucine (3%), challenging the concept that translational ambiguity has a negative impact in living organisms. To elucidate the molecular mechanisms underlying the in vivo tolerance to a nonconserved genetic code alteration, we have undertaken an extensive structural analysis of proteins containing CUG-encoded residues and solved the crystal structures of the two natural isoforms of\n            <jats:italic>Candida albicans<\/jats:italic>\n            seryl-tRNA synthetase. We show that codon reassignment resulted in a nonrandom genome-wide CUG redistribution tailored to minimize protein misfolding events induced by the large-scale leucine-to-serine replacement within the CTG clade. Leucine or serine incorporation at the CUG position in\n            <jats:italic>C. albicans<\/jats:italic>\n            seryl-tRNA synthetase induces only local structural changes and, although both isoforms display tRNA serylation activity, the leucine-containing isoform is more active. Similarly, codon ambiguity is predicted to shape the function of\n            <jats:italic>C. albicans<\/jats:italic>\n            proteins containing CUG-encoded residues in functionally relevant positions, some of which have a key role in signaling cascades associated with morphological changes and pathogenesis. This study provides a first detailed analysis on natural reassignment of codon identity, unveiling a highly dynamic evolutionary pattern of thousands of fungal CUG codons to confer an optimized balance between protein structural robustness and functional plasticity.\n          <\/jats:p>","DOI":"10.1073\/pnas.1102835108","type":"journal-article","created":{"date-parts":[[2011,8,9]],"date-time":"2011-08-09T06:20:00Z","timestamp":1312870800000},"page":"14091-14096","update-policy":"http:\/\/dx.doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":42,"title":["Unveiling the structural basis for translational ambiguity tolerance in a human fungal pathogen"],"prefix":"10.1073","volume":"108","author":[{"given":"Rita","family":"Rocha","sequence":"first","affiliation":[{"name":"Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, 4150-180 Porto, Portugal; and"},{"name":"RNA Biology Laboratory, Department of Biology and Centre for Environmental and Marine Studies (CESAM), University of Aveiro, 3810-193 Aveiro, Portugal"}]},{"given":"Pedro Jos\u00e9 Barbosa","family":"Pereira","sequence":"additional","affiliation":[{"name":"Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, 4150-180 Porto, Portugal; and"}]},{"given":"Manuel A. 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