ArticleMetabolic engineering2012
Multi-copy genes that enhance the yield of mammalian G protein-coupled receptors in Escherichia coli.
Article in Metabolic engineering, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- A previously unidentified sugar transporter for engineering of high-yield Streptomyces.Applied microbiology and biotechnology · 2024Article
- Escherichia coli strains with precise domain deletions in the ribonuclease RNase E can achieve greatly enhanced levels of membrane protein production.Protein science : a publication of the Protein Society · 2024Article
- Glucose consumption rate-dependent transcriptome profiling of Escherichia coli provides insight on performance as microbial factories.Microbial cell factories · 2022Article
- Second-GenerationACS synthetic biology · 2022Article
- High-throughput cell-free screening of eukaryotic membrane protein expression in lipidic mimetics.Protein science : a publication of the Protein Society · 2022Article
- Increased Synthesis of a Magnesium Transporter MgtA During Recombinant Autotransporter Expression in Escherichia coli.Applied biochemistry and biotechnology · 2021Article
- Smoothing membrane protein structure determination by initial upstream stage improvements.Applied microbiology and biotechnology · 2019Review
- High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives.Open biology · 2016Review
- Engineering therapeutic antibodies targeting G-protein-coupled receptors.Experimental & molecular medicine · 2016Review
- Escherichia coli as host for membrane protein structure determination: a global analysis.Scientific reports · 2015Article
- Recombinant polypeptide production in E. coli: towards a rational approach to improve the yields of functional proteins.Microbial cell factories · 2013Review
- Combinatorial approaches for inverse metabolic engineering applications.Computational and structural biotechnology journal · 2012Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Low yields of recombinant expression represent a major barrier to the physical characterization of membrane proteins. Here, we have identified genes that globally enhance the production of properly folded G protein-coupled receptors (GPCRs) in Escherichia coli. Libraries of bacterial chromosomal fragments were screened using two separate systems that monitor: (i) elevated fluorescence conferred by enhanced expression of GPCR-GFP fusions and (ii) increased binding of fluorescent ligand in cells producing more active receptor. Three multi-copy hits were isolated by both methods: nagD, encoding the ribonucleotide phosphatase NagD; a fragment of nlpD, encoding a truncation of the predicted lipoprotein NlpD, and the three-gene cluster ptsN-yhbJ-npr, encoding three proteins of the nitrogen phosphotransferase system. Expression of these genes resulted in a 3- to 10-fold increase in the yields of different mammalian GPCRs. Our data is consistent with the hypothesis that the expression of these genes may serve to maintain the integrity of the bacterial periplasm and to provide a favorable environment for proper membrane protein folding, possibly by inducing a fine-tuned stress response and/or via modifying the composition of the bacterial cell envelope.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.