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Production of Membrane Proteins in Pseudomonas stutzeri

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Xie,  Hao
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Münke,  Cornelia
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Sommer,  Manuel
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Buschmann,  Sabine
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Michel,  Hartmut
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Xie, H., Münke, C., Sommer, M., Buschmann, S., & Michel, H. (2022). Production of Membrane Proteins in Pseudomonas stutzeri. In I. Mus-Veteau (Ed.), Methods in Molecular Biology (pp. 91-110). New York, NY: Humana Press. doi:10.1007/978-1-0716-2368-8_6.


Cite as: http://hdl.handle.net/21.11116/0000-000A-AAC5-8
Abstract
Functional and structural studies on membrane proteins are often hampered by insufficient yields, misfolding and aggregation during the production and purification process. Escherichia coli is the most commonly used expression host for the production of recombinant prokaryotic integral membrane proteins. However, in many cases expression hosts other than E. coli are more appropriate for certain target proteins. Here, we report a convenient, systematically developed expression system using the γ-proteobacterium Pseudomonas stutzeri as an alternative production host for over-expression of integral membrane proteins. P. stutzeri can be easily and inexpensively cultured in large quantities. The Pseudomonas expression vectors are designed for inducible expression of affinity-tagged fusion proteins controlled by the PBAD promoter. This chapter provides detailed protocols of the different steps required to successfully produce and isolate recombinant membrane proteins with high yields in P. stutzeri.