ArticleProtein science : a publication of the Protein Society2007
Cell-free complements in vivo expression of the E. coli membrane proteome.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Reversible Control of Gene Expression by Guest-Modified Adenosines in a Cell-Free System via Host-Guest Interaction.Journal of the American Chemical Society · 2024Article
- High-throughput cell-free screening of eukaryotic membrane protein expression in lipidic mimetics.Protein science : a publication of the Protein Society · 2022Article
- Structure formation during translocon-unassisted co-translational membrane protein folding.Scientific reports · 2017Article
- Cell-free expression and in meso crystallisation of an integral membrane kinase for structure determination.Cellular and molecular life sciences : CMLS · 2014Article
- A continuous-exchange cell-free protein synthesis system based on extracts from cultured insect cells.PloS one · 2014Article
- Detergent/nanodisc screening for high-resolution NMR studies of an integral membrane protein containing a cytoplasmic domain.PloS one · 2013Article
- Facile backbone structure determination of human membrane proteins by NMR spectroscopy.Nature methods · 2012Article
- Cotranslational cis-phosphorylation of the COOH-terminal tail is a key priming step in the maturation of cAMP-dependent protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Article
- Functional expression of the PorAH channel from Corynebacterium glutamicum in cell-free expression systems: implications for the role of the naturally occurring mycolic acid modification.The Journal of biological chemistry · 2011Article
- High throughput platforms for structural genomics of integral membrane proteins.Current opinion in structural biology · 2011Review
- Polymer-based cell-free expression of ligand-binding family B G-protein coupled receptors without detergents.Protein science : a publication of the Protein Society · 2011Article
- Designer lipid-like peptides: a class of detergents for studying functional olfactory receptors using commercial cell-free systems.PloS one · 2011Article
- A robust and rapid method of producing soluble, stable, and functional G-protein coupled receptors.PloS one · 2011Article
- Revolutionizing membrane protein overexpression in bacteria.Microbial biotechnology · 2010Review
- Sugar (ribose), spice (peroxidase) and all things nice (laccase hair-dyes).Microbial biotechnology · 2010Article
- A general protocol for the crystallization of membrane proteins for X-ray structural investigation.Nature protocols · 2009Article
- Efficient cell-free production of olfactory receptors: detergent optimization, structure, and ligand binding analyses.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Functional protein expression from a DNA based wheat germ cell-free system.Journal of structural and functional genomics · 2007Article
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5 authors.
Funding
Abstract
Reconstituted cell-free (CF) protein expression systems hold the promise of overcoming the traditional barriers associated with in vivo systems. This is particularly true for membrane proteins, which are often cytotoxic and due to the nature of the membrane, difficult to work with. To evaluate the potential of cell-free expression, we cloned 120 membrane proteins from E. coli and compared their expression profiles in both an E. coli in vivo system and an E. coli-derived cell-free system. Our results indicate CF is a more robust system and we were able to express 63% of the targets in CF, compared to 44% in vivo. To benchmark the quality of CF produced protein, five target membrane proteins were purified and their homogeneity assayed by gel filtration chromatography. Finally, to demonstrate the ease of amino acid labeling with CF, a novel membrane protein was substituted with selenomethionine, purified, and shown to have 100% incorporation of the unnatural amino acid. We conclude that CF is a novel, robust expression system capable of expressing more proteins than an in vivo system and suitable for production of membrane proteins at the milligram level.
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