ArticleProtein science : a publication of the Protein Society2010
A rapid protein folding assay for the bacterial periplasm.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
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- High-throughput developability assays enable library-scale identification of producible protein scaffold variants.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Production and Sensing of Butyrate in a ProbioticInternational journal of molecular sciences · 2020Article
- Development of a generic β-lactamase screening system for improved signal peptides for periplasmic targeting of recombinant proteins in Escherichia coli.Scientific reports · 2018Article
- Evaluating a New High-throughput Twin-Arginine Translocase Assay in Bacteria for Therapeutic Applications.Current microbiology · 2017Article
- A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.Nature communications · 2017Article
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- Multiple driving forces required for efficient secretion of autotransporter virulence proteins.The Journal of biological chemistry · 2015Article
- An alternative outer membrane secretion mechanism for an autotransporter protein lacking a C-terminal stable core.Molecular microbiology · 2013Article
- Article
- Molecular insights into the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1.FEBS letters · 2012Review
- Techniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living Cells.The Korean journal of chemical engineering · 2012Article
- The ribosomal exit tunnel as a target for optimizing protein expression in Escherichia coli.Biotechnology journal · 2012Article
- Protein folding in the cell: challenges and progress.Current opinion in structural biology · 2011Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An array of genetic screens and selections has been developed for reporting protein folding and solubility in the cytoplasm of living cells. However, there are currently no analogous folding assays for the bacterial periplasm, despite the significance of this compartment for the expression of recombinant proteins, especially those requiring important posttranslational modifications (e.g., disulfide bond formation). Here, we describe an engineered genetic selection for monitoring protein folding in the periplasmic compartment of Escherichia coli cells. In this approach, target proteins are sandwiched between an N-terminal signal recognition particle (SRP)-dependent signal peptide and a C-terminal selectable marker, TEM-1 beta-lactamase. The resulting chimeras are localized to the periplasmic space via the cotranslational SRP pathway. Using a panel of native and heterologous proteins, we demonstrate that the folding efficiency of various target proteins correlates directly with in vivo beta-lactamase activity and thus resistance to ampicillin. We also show that this reporter is useful for the discovery of extrinsic periplasmic factors (e.g., chaperones) that affect protein folding and for obtaining folding-enhanced proteins via directed evolution. Collectively, these data demonstrate that our periplasmic folding reporter is a powerful tool for screening and engineering protein folding in a manner that does not require any structural or functional information about the target protein.
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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.