Functional characterization of a highly specific L-arabinose transporter from Trichoderma reesei
| Autor: | Havukainen, Sami, Pujol-Gim��nez, Jonai, Valkonen, Mari, Hediger, Matthias, Landowski, Christopher P |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
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| Zdroj: | Havukainen, Sami; Pujol-Giménez, Jonai; Valkonen, Mari; Hediger, Matthias; Landowski, Christopher P (2021). Functional characterization of a highly specific L-arabinose transporter from Trichoderma reesei. Microbial cell factories, 20(1), p. 177. BioMed Central 10.1186/s12934-021-01666-4 Microbial Cell Factories, Vol 20, Iss 1, Pp 1-20 (2021) Havukainen, S, Pujol-Giménez, J, Valkonen, M, Hediger, M A & Landowski, C P 2021, ' Functional characterization of a highly specific l-arabinose transporter from Trichoderma reesei ', Microbial Cell Factories, vol. 20, 177 . https://doi.org/10.1186/s12934-021-01666-4 Microbial Cell Factories |
| DOI: | 10.1186/s12934-021-01666-4 |
| Popis: | Background Lignocellulose biomass has been investigated as a feedstock for second generation biofuels and other value-added products. Some of the processes for biofuel production utilize cellulases and hemicellulases to convert the lignocellulosic biomass into a range of soluble sugars before fermentation with microorganisms such as yeast Saccharomyces cerevisiae. One of these sugars is l-arabinose, which cannot be utilized naturally by yeast. The first step in l-arabinose catabolism is its transport into the cells, and yeast lacks a specific transporter, which could perform this task. Results We identified Trire2_104072 of Trichoderma reesei as a potential l-arabinose transporter based on its expression profile. This transporter was described already in 2007 as d-xylose transporter XLT1. Electrophysiology experiments with Xenopus laevis oocytes and heterologous expression in yeast revealed that Trire2_104072 is a high-affinity l-arabinose symporter with a Km value in the range of \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\sim$$\end{document}∼ 0.1–0.2 mM. It can also transport d-xylose but with low affinity (Km \documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}$$\sim$$\end{document}∼ 9 mM). In yeast, l-arabinose transport was inhibited slightly by d-xylose but not by d-glucose in an assay with fivefold excess of the inhibiting sugar. Comparison with known l-arabinose transporters revealed that the expression of Trire2_104072 enabled yeast to uptake l-arabinose at the highest rate in conditions with low extracellular l-arabinose concentration. Despite the high specificity of Trire2_104072 for l-arabinose, the growth of its T. reesei deletion mutant was only affected at low l-arabinose concentrations. Conclusions Due to its high affinity for l-arabinose and low inhibition by d-glucose or d-xylose, Trire2_104072 could serve as a good candidate for improving the existing pentose-utilizing yeast strains. The discovery of a highly specific l-arabinose transporter also adds to our knowledge of the primary metabolism of T. reesei. The phenotype of the deletion strain suggests the involvement of other transporters in l-arabinose transport in this species. Supplementary Information The online version contains supplementary material available at 10.1186/s12934-021-01666-4. |
| Databáze: | OpenAIRE |
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