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.
Highlights
We have seen amazing advances in the field of membrane protein research over the past four years
Once again this study demonstrated that slowing down transcription is one key to success for membrane protein biogenesis
Published work provides insights into the mechanisms of membrane protein biogenesis so that many useful guidelines, hints and tips are available enabling us to improve the design of future experiments
Summary
We have seen amazing advances in the field of membrane protein research over the past four years. Many years of strenuous efforts were required to get the proteins to crystals, relying on iterative optimization of all steps from expression to purification and crystallization. The total number of membrane protein structures deposited in the protein data bank (PDB) strikingly reflects that membrane protein research can not yet keep pace with the one of soluble proteins. The discrepancy between biodiversity and poor structural knowledge can be largely attributed to the low natural expression of membrane proteins, to their hydrophobic character which complicates overexpression of functional membrane proteins, as well as to difficulties during their purification and crystallization.
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