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  • Artificial Self-assembling Nanocompartment for Organizing Metabolic Pathways in Yeast

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    Sainsbury514488-Published.pdf (5.636Mb)
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    Version of Record (VoR)
    Author(s)
    Cheah, Li Chen
    Stark, Terra
    Adamson, Lachlan SR
    Abidin, Rufika S
    Lau, Yu Heng
    Sainsbury, Frank
    Vickers, Claudia E
    Griffith University Author(s)
    Sainsbury, Frank
    Vickers, Claudia E.
    Year published
    2021
    Metadata
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    Abstract
    Metabolic pathways are commonly organized by sequestration into discrete cellular compartments. Compartments prevent unfavorable interactions with other pathways and provide local environments conducive to the activity of encapsulated enzymes. Such compartments are also useful synthetic biology tools for examining enzyme/pathway behavior and for metabolic engineering. Here, we expand the intracellular compartmentalization toolbox for budding yeast (Saccharomyces cerevisiae) with Murine polyomavirus virus-like particles (MPyV VLPs). The MPyV system has two components: VP1 which self-assembles into the compartment shell and a ...
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    Metabolic pathways are commonly organized by sequestration into discrete cellular compartments. Compartments prevent unfavorable interactions with other pathways and provide local environments conducive to the activity of encapsulated enzymes. Such compartments are also useful synthetic biology tools for examining enzyme/pathway behavior and for metabolic engineering. Here, we expand the intracellular compartmentalization toolbox for budding yeast (Saccharomyces cerevisiae) with Murine polyomavirus virus-like particles (MPyV VLPs). The MPyV system has two components: VP1 which self-assembles into the compartment shell and a short anchor, VP2C, which mediates cargo protein encapsulation via binding to the inner surface of the VP1 shell. Destabilized green fluorescent protein (GFP) fused to VP2C was specifically sorted into VLPs and thereby protected from host-mediated degradation. An engineered VP1 variant displayed improved cargo capture properties and differential subcellular localization compared to wild-type VP1. To demonstrate their ability to function as a metabolic compartment, MPyV VLPs were used to encapsulate myo-inositol oxygenase (MIOX), an unstable and rate-limiting enzyme in d-glucaric acid biosynthesis. Strains with encapsulated MIOX produced ∼20% more d-glucaric acid compared to controls expressing "free" MIOX-despite accumulating dramatically less expressed protein-and also grew to higher cell densities. This is the first demonstration in yeast of an artificial biocatalytic compartment that can participate in a metabolic pathway and establishes the MPyV platform as a promising synthetic biology tool for yeast engineering.
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    Journal Title
    ACS Synthetic Biology
    DOI
    https://doi.org/10.1021/acssynbio.1c00045
    Copyright Statement
    © The Author(s) 2021. This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International (CC BY-NC-ND 4.0) License, which permits unrestricted, non-commercial use, distribution and reproduction in any medium, providing that the work is properly cited.
    Note
    This publication has been entered in Griffith Research Online as an advanced online version.
    Subject
    Medicinal and biomolecular chemistry
    Biomedical engineering
    Macromolecular and materials chemistry
    Biochemistry and cell biology
    glucaric acid
    metabolic engineering
    nanocompartment
    polyomavirus
    virus-like particles
    Publication URI
    http://hdl.handle.net/10072/408553
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    • Journal articles

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