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Heterologous Expression of Membrane Proteins in E. coli

Authors :
Peer, Depping
María Monserrat, Román Lara
Athanasios, Kesidis
Roslyn M, Bill
Alice J, Rothnie
Douglas F, Browning
Alan D, Goddard
Source :
Methods in molecular biology (Clifton, N.J.). 2507
Publication Year :
2022

Abstract

Over the decades, the bacterium Escherichia coli (E. coli) has become the cornerstone of recombinant protein production, used for heterologous synthesis of a variety of membrane proteins. Due to its rapid growth to high densities in cheap media, and its ease of manipulation and handling, E. coli is an excellent host cell for a range of membrane protein targets. Furthermore, its genetic tractability allows for a variety of gene constructs to be screened for optimal expression conditions, resulting in relatively high yields of membrane protein in a short amount of time. Here, we describe the general workflow for the production of membrane proteins in E. coli. The protocols we provide show how the gene of interest is modified, transferred to an expression vector and host, and how membrane protein yields can be optimized and analyzed. The examples we illustrate are well suited for scientists who are starting their journey into the world of membrane protein production.

Details

ISSN :
19406029
Volume :
2507
Database :
OpenAIRE
Journal :
Methods in molecular biology (Clifton, N.J.)
Accession number :
edsair.pmid..........e61c08da6677715f8338153572ac9aeb