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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 Ca 2+ /Mn 2+  ATPase. Deleting  PMR1  in the parental XI-expressing strain enabled instantaneous anaerobic growth on  d -xylose. In  pmr1  strains, intracellular Mn 2+  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 Mn 2+  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.

scientific reports

Mutations in PMR1 stimulate xylose isomerase activity and anaerobic growth on xylose of engineered Saccharomyces cerevisiae by influencing manganese homeostasis