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    Side effects of chaperone gene co-expression in recombinant protein production

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    Authors
    Martínez-Alonso, Mónica
    García-Fruitós, Elena
    Ferrer-Miralles, Neus
    Rinas, Ursula
    Villaverde, Antonio
    Issue Date
    2010-09-02
    
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    Abstract
    Abstract Insufficient availability of molecular chaperones is observed as a major bottleneck for proper protein folding in recombinant protein production. Therefore, co-production of selected sets of cell chaperones along with foreign polypeptides is a common approach to increase the yield of properly folded, recombinant proteins in bacterial cell factories. However, unbalanced amounts of folding modulators handling folding-reluctant protein species might instead trigger undesired proteolytic activities, detrimental regarding recombinant protein stability, quality and yield. This minireview summarizes the most recent observations of chaperone-linked negative side effects, mostly focusing on DnaK and GroEL sets, when using these proteins as folding assistant agents. These events are discussed in the context of the complexity of the cell quality network and the consequent intricacy of the physiological responses triggered by protein misfolding.
    Citation
    Microbial Cell Factories. 2010 Sep 02;9(1):64
    URI
    http://dx.doi.org/10.1186/1475-2859-9-64
    http://hdl.handle.net/10033/620788
    Type
    Journal Article
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    Publications of the research group structure and functions of Proteins(SFPR)

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