Tuning microbial hosts for membrane protein production. Microb Cell Fact 8:69

Institute of Molecular Biotechnology, Graz University of Technology, Petersgasse 14, 8010 Graz, Austria.
Microbial Cell Factories (Impact Factor: 4.25). 12/2009; 8:69. DOI: 10.1186/1475-2859-8-69
Source: PubMed

ABSTRACT The last four years have brought exciting progress in membrane protein research. Finally those many efforts that have been put into expression of eukaryotic membrane proteins are coming to fruition and enable to solve an ever-growing number of high resolution structures. In the past, many skilful optimization steps were required to achieve sufficient expression of functional membrane proteins. Optimization was performed individually for every membrane protein, but provided insight about commonly encountered bottlenecks and, more importantly, general guidelines how to alleviate cellular limitations during microbial membrane protein expression. Lately, system-wide analyses are emerging as powerful means to decipher cellular bottlenecks during heterologous protein production and their use in microbial membrane protein expression has grown in popularity during the past months.
This review covers the most prominent solutions and pitfalls in expression of eukaryotic membrane proteins using microbial hosts (prokaryotes, yeasts), highlights skilful applications of our basic understanding to improve membrane protein production. Omics technologies provide new concepts to engineer microbial hosts for membrane protein production.

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Available from: Anton Glieder, Aug 18, 2015
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    • "Because membrane proteins are found in their natural cellular environments in quantities that are too low for biochemical analysis, they have to be prepared by expression in heterologous hosts (Link and Georgiou, 2007; Wagner et al., 2006). Escherichia coli have been by far the most successful host for the preparative expression of heterologous membrane proteins (Freigassner et al., 2009; Wagner et al., 2006). Unfortunately, many mammalian membrane proteins fail to form correctly in bacteria and instead accumulate as cytoplasmic inclusion bodies that are very difficult to refold (Link and Georgiou, 2007). "
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