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  • The Targeted Expression of Nucleotide Sugar Transporters to the E. coli Inner Membrane

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    Author(s)
    Tiralongo, Joe
    Maggioni, Andrea
    Griffith University Author(s)
    Maggioni, Andrea
    Tiralongo, Joe
    Year published
    2011
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    Abstract
    The heterologous expression of functional mammalian integral membrane proteins still represents a significant hurdle towards evaluating the relationship between their structure and function. We have therefore utilised the OmpA signal sequence to deliberately target the expression of a mammalian nucleotide sugar transporter, the murine CMP-sialic acid transporter, to the E. coli inner membrane. The functionality of the recombinant CMP-sialic acid transporter could then be evaluated either following the spheroplasting of E. coli cells or through the isolation of the E. coli inner membrane and the formation of mixed ...
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    The heterologous expression of functional mammalian integral membrane proteins still represents a significant hurdle towards evaluating the relationship between their structure and function. We have therefore utilised the OmpA signal sequence to deliberately target the expression of a mammalian nucleotide sugar transporter, the murine CMP-sialic acid transporter, to the E. coli inner membrane. The functionality of the recombinant CMP-sialic acid transporter could then be evaluated either following the spheroplasting of E. coli cells or through the isolation of the E. coli inner membrane and the formation of mixed phosphatidylcholine-inner membrane proteoliposomes.
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    Journal Title
    Methods in Molecular Biology
    Volume
    705
    DOI
    https://doi.org/10.1007/978-1-61737-967-3_14
    Copyright Statement
    © 2011 Springer. This is an electronic version of an article published in Methods in Molecular Biology, Vol. 705, 2011, pp. 237-249. Methods in Molecular Biology is available online at: http://link.springer.com// with the open URL of your article.
    Subject
    Other chemical sciences
    Biochemistry and cell biology
    Receptors and membrane biology
    Publication URI
    http://hdl.handle.net/10072/43425
    Collection
    • Journal articles

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