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Affibody Scaffolds Improve Sesquiterpene Production in Saccharomyces cerevisiae

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† Department of Biology and Biological Engineering, Chalmers University of Technology, SE412 96 Gothenburg, Sweden
‡ Novo Nordisk Foundation Center for Biosustainability, Chalmers University of Technology, SE412 96 Gothenburg, Sweden
§ Division of Proteomics and Nanobiotechnology, School of Biotechnology, Royal Institute of Technology (KTH), Science for Life Laboratory, SE171 21 Stockholm, Sweden
∥ Department of Chemical and Biological Engineering, University of Wisconsin−Madison, Madison, Wisconsin 53706, United States
⊥ Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, DK2970 Hørsholm, Denmark
*E-mail: [email protected]. Tel: +46 8 553 783 17.
Cite this: ACS Synth. Biol. 2017, 6, 1, 19–28
Publication Date (Web):August 25, 2016
https://doi.org/10.1021/acssynbio.6b00109
Copyright © 2016 American Chemical Society
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    Abstract

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    Enzyme fusions have been widely used as a tool in metabolic engineering to increase pathway efficiency by reducing substrate loss and accumulation of toxic intermediates. Alternatively, enzymes can be colocalized through attachment to a synthetic scaffold via noncovalent interactions. Here we describe the use of affibodies for enzyme tagging and scaffolding. The scaffolding is based on the recognition of affibodies to their anti-idiotypic partners in vivo, and was first employed for colocalization of farnesyl diphosphate synthase and farnesene synthase in S. cerevisiae. Different parameters were modulated to improve the system, and the enzyme:scaffold ratio was most critical for its functionality. Ultimately, the yield of farnesene on glucose YSFar could be improved by 135% in fed-batch cultivations using a 2-site affibody scaffold. The scaffolding strategy was then extended to a three-enzyme polyhydroxybutyrate (PHB) pathway, heterologously expressed in E. coli. Within a narrow range of enzyme and scaffold induction, the affibody tagging and scaffolding increased PHB production 7-fold. This work demonstrates how the versatile affibody can be used for metabolic engineering purposes.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/acssynbio.6b00109.

    • Oligonucleotide primers used for chromosomal integration in S. cerevisiae and plasmid construction (Table S1 and S2), nucleotide sequences of all affibodies, scaffold effect on farnesene production using single plasmid expression (Figure S1), negative control experiment (Figure S2), effect of linker length and carbon source on affibody scaffolding (Figure S3), farnesene yield on glucose and final farnesene titers obtained in fed-batch cultivations when scaffold is expressed from PTEF1, Western Blot detection of Z-fused enzymes and affibody scaffold (Figure S5), Effect of scaffold expression of PHB production in LB media (Figure S6), schematic representation of putative colocalization mediated by affibodies (Figure S7) (PDF)

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