Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/74378

TítuloEvolutionary engineering reveals amino acid substitutions in Ato2 and Ato3 that allow improved growth of Saccharomyces cerevisiae on lactic acid
Autor(es)Baldi, Nicolò
de Valk, Sophie Claire
Sousa-Silva, M.
Casal, Margarida
Soares-Silva, Isabel João
Mans, Robert
Palavras-chaveYeast
Carboxylate transporters
Biotechnology
Evolutionary engineering
Transport
Protein structure
Reverse engineering
Carboxylic acids
DataMai-2021
EditoraFederation of European Microbiological Societies
RevistaFEMS Yeast Research
CitaçãoBaldi, N., de Valk, S. C., Sousa-Silva, M., Casal, M., Soares-Silva, I., & Mans, R. (2021). Evolutionary engineering reveals amino acid substitutions in Ato2 and Ato3 that allow improved growth of Saccharomyces cerevisiae on lactic acid. FEMS Yeast Research, 21(4)
Resumo(s)In Saccharomyces cerevisiae, the complete set of proteins involved in transport of lactic acid across the cell membrane has not been determined. In this study we aimed to identify transport proteins not previously described to be involved in lactic acid transport via a combination of directed evolution, whole-genome resequencing and reverse engineering. Evolution of a strain lacking all known lactic acid transporters on lactate led to the discovery of mutated Ato2 and Ato3 as two novel lactic acid transport proteins. When compared to previously identified S. cerevisiae genes involved in lactic acid transport, expression of ATO3T284C was able to facilitate the highest growth rate (0.15 ± 0.01 h-1) on this carbon source. A comparison between (evolved) sequences and 3D models of the transport proteins showed that most of the identified mutations resulted in a widening of the narrowest hydrophobic constriction of the anion channel. We hypothesize that this observation, sometimes in combination with an increased binding affinity of lactic acid to the sites adjacent to this constriction, are responsible for the improved lactic acid transport in the evolved proteins.
TipoArtigo
URIhttps://hdl.handle.net/1822/74378
DOI10.1093/femsyr/foab033
ISSN1567-1356
e-ISSN1567-1364
Versão da editorahttps://academic.oup.com/femsyr/article-abstract/21/4/foab033/6286924
Arbitragem científicayes
AcessoAcesso aberto
Aparece nas coleções:CBMA - Artigos/Papers

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