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Anaerobic alpha-Amylase Production and Secretion with Fumarate as the Final Electron Acceptor in Saccharomyces cerevisiae

Journal article
Authors Zihe Liu
Tobias Österlund
Jin Hou
Dina Petranovic
Jens B. Nielsen
Published in Applied and Environmental Microbiology
Volume 79
Issue 9
Pages 2962-2967
ISSN 0099-2240
Publication year 2013
Published at
Pages 2962-2967
Language en
Keywords disulfide bond formation, endoplasmic-reticulum, recombinant proteins, systems biology, stress, yeast, eukaryotes, ero1p, degradation, metabolism
Subject categories Chemical Sciences

Abstract

In this study, we focus on production of heterologous alpha-amylase in the yeast Saccharomyces cerevisiae under anaerobic conditions. We compare the metabolic fluxes and transcriptional regulation under aerobic and anaerobic conditions, with the objective of identifying the final electron acceptor for protein folding under anaerobic conditions. We find that yeast produces more amylase under anaerobic conditions than under aerobic conditions, and we propose a model for electron transfer under anaerobic conditions. According to our model, during protein folding the electrons from the endoplasmic reticulum are transferred to fumarate as the final electron acceptor. This model is supported by findings that the addition of fumarate under anaerobic (but not aerobic) conditions improves cell growth, specifically in the alpha-amylase-producing strain, in which it is not used as a carbon source. Our results provide a model for the molecular mechanism of anaerobic protein secretion using fumarate as the final electron acceptor, which may allow for further engineering of yeast for improved protein secretion under anaerobic growth conditions.

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