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• W2050687416 abstract "The major barrier to the physical characterization and structure determination of membrane proteins is low protein yield and/or low functionality in recombinant expression. The enteric bacterium Escherichia coli is the most widely employed organism for producing recombinant proteins . Beside several advantages of this expression host, one major drawback is that the protein of interest does not always adopt its native conformation and may end up in large insoluble aggregates. We describe a robust strategy to increase the likelihood of overexpressing membrane proteins in a functional state. The method involves fusion in tandem of green fluorescent protein and the erythromycin resistance protein (23S ribosomal RNA adenine N -6 methyltransferase , ErmC) to the C-terminus of a target membrane protein. The fluorescence of green fluorescent protein is used to report the folding state of the target protein, whereas ErmC is used to select for increased expression. By gradually increasing the erythromycin concentration of the medium and testing different membrane protein targets, we obtained a number of evolved strains of which four (NG2, NG3, NG5 and NG6) were characterized and their genome was fully sequenced. Strikingly, each of the strains carried a mutation in the hns gene, whose product is involved in genome organization and transcriptional silencing. The degree of expression of (membrane) proteins correlates with the severity of the hns mutation, but cells in which hns was deleted showed an intermediate expression performance. We propose that (partial) removal of the transcriptional silencing mechanism changes the levels of proteins essential for the functional overexpression of membrane proteins. • We present a method to improve the functional expression of membrane proteins. • Genome sequencing identifies genes that modulate membrane protein expression. • Mutations in hns increase membrane protein production. • We present new insight into factors that limit the biogenesis of membrane proteins." @default.
• W2050687416 created "2016-06-24" @default.
• W2050687416 creator A5037378658 @default.
• W2050687416 creator A5041070000 @default.
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• W2050687416 creator A5064895339 @default.
• W2050687416 date "2014-01-01" @default.
• W2050687416 modified "2023-10-11" @default.
• W2050687416 title "Evolved Escherichia coli Strains for Amplified, Functional Expression of Membrane Proteins" @default.
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• W2050687416 doi "https://doi.org/10.1016/j.jmb.2013.09.009" @default.
• W2050687416 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24041572" @default.
• W2050687416 hasPublicationYear "2014" @default.
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