Revolutionizing membrane protein overexpression in bacteria
Article first published online: 4 SEP 2009
© 2009 The Authors. Journal compilation © 2009 Society for Applied Microbiology and Blackwell Publishing Ltd
Volume 3, Issue 4, pages 403–411, July 2010
How to Cite
Schlegel, S., Klepsch, M., Gialama, D., Wickström, D., Slotboom, D. J. and De Gier, J.-W. (2010), Revolutionizing membrane protein overexpression in bacteria. Microbial Biotechnology, 3: 403–411. doi: 10.1111/j.1751-7915.2009.00148.x
- Issue published online: 24 JUN 2010
- Article first published online: 4 SEP 2009
- Received 1 April 2009; revised 30 July 2009; accepted 30 July 2009.
The bacterium Escherichia coli is the most widely used expression host for overexpression trials of membrane proteins. Usually, different strains, culture conditions and expression regimes are screened for to identify the optimal overexpression strategy. However, yields are often not satisfactory, especially for eukaryotic membrane proteins. This has initiated a revolution of membrane protein overexpression in bacteria. Recent studies have shown that it is feasible to (i) engineer or select for E. coli strains with strongly improved membrane protein overexpression characteristics, (ii) use bacteria other than E. coli for the expression of membrane proteins, (iii) engineer or select for membrane protein variants that retain functionality but express better than the wild-type protein, and (iv) express membrane proteins using E. coli-based cell-free systems.