The targeted expression of nucleotide sugar transporters to the E. coli inner membrane.
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.
Institute for Glycomics, Griffith University, Southport, QLD, Australia. j.tiralongo@griffith.edu.au
Joe
J
Tiralongo
Andrea
A
Maggioni
D000818:Animals; D001425:Bacterial Outer Membrane Proteins; D002462:Cell Membrane / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D051379:Mice; D027361:Organic Anion Transporters / Q000096:biosynthesis* / Q000235:genetics; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000235:genetics; D027981:Symporters / Q000096:biosynthesis* / Q000235:genetics
D001425:Bacterial Outer Membrane Proteins; D027361:Organic Anion Transporters; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D027981:Symporters; C421224:sialic acid transport proteins; C078167:OMPA outer membrane proteins