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Mutations in PMR1 stimulate xylose isomerase activity and anaerobic growth on xylose of engineered Saccharomyces cerevisiae by influencing manganese homeostasis
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2017 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 7, article id 46155Article in journal (Refereed) Published
Abstract [en]

Combined overexpression of xylulokinase, pentose-phosphate-pathway enzymes and a heterologous xylose isomerase (XI) is required but insufficient for anaerobic growth of Saccharomyces cerevisiae on d-xylose. Single-step Cas9-assisted implementation of these modifications yielded a yeast strain expressing Piromyces XI that showed fast aerobic growth on d-xylose. However, anaerobic growth required a 12-day adaptation period. Xylose-adapted cultures carried mutations in PMR1, encoding a Golgi Ca2+/Mn2+ ATPase. Deleting PMR1 in the parental XI-expressing strain enabled instantaneous anaerobic growth on d-xylose. In pmr1 strains, intracellular Mn2+ concentrations were much higher than in the parental strain. XI activity assays in cell extracts and reconstitution experiments with purified XI apoenzyme showed superior enzyme kinetics with Mn2+ relative to other divalent metal ions. This study indicates engineering of metal homeostasis as a relevant approach for optimization of metabolic pathways involving metal-dependent enzymes. Specifically, it identifies metal interactions of heterologous XIs as an underexplored aspect of engineering xylose metabolism in yeast.

Place, publisher, year, edition, pages
Nature Publishing Group, 2017. Vol. 7, article id 46155
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Biological Sciences
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URN: urn:nbn:se:kth:diva-206684DOI: 10.1038/srep46155ISI: 000398987300001PubMedID: 28401919Scopus ID: 2-s2.0-85017464092OAI: oai:DiVA.org:kth-206684DiVA, id: diva2:1094454
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QC 20170510

Available from: 2017-05-10 Created: 2017-05-10 Last updated: 2017-12-05Bibliographically approved

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van Maris, Antonius J. A.

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