ArticleProtein science : a publication of the Protein Society2006
Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 118 citations in OpenAlex.
- Tat-dependent protein translocation and its evolution.FEMS microbiology reviews · 2026Review
- SAS: Split antibiotic selection for identifying chaperones that improve protein solubility.Heliyon · 2024Article
- Isolation of full-length IgG antibodies from combinatorial libraries expressed in the cytoplasm of Escherichia coli.Nature communications · 2023Article
- Experimental characterization of de novo proteins and their unevolved random-sequence counterparts.Nature ecology & evolution · 2023Article
- Design of an artificial phage-display library based on a new scaffold improved for average stability of the randomized proteins.Scientific reports · 2023Article
- Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity.Scientific reports · 2022Article
- Two-Tiered Selection and Screening Strategy to Increase Functional Enzyme Production in E. coli.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Prediction of Residue-specific Contributions to Binding and Thermal Stability Using Yeast Surface Display.Frontiers in molecular biosciences · 2021Article
- Directed evolution methods for overcoming trade-offs between protein activity and stability.AIChE journal. American Institute of Chemical Engineers · 2020Article
- Determination of melatonin by a whole cell bioassay in fermented beverages.Scientific reports · 2019Article
- Characterization of a novel method for the production of single-span membrane proteins in Escherichia coli.Biotechnology and bioengineering · 2019Article
- Selection of Protein-Protein Interactions of Desired Affinities with a Bandpass Circuit.Journal of molecular biology · 2019Article
- Directed evolution to improve protein folding in vivo.Current opinion in structural biology · 2018Review
- Trade-offs between enzyme fitness and solubility illuminated by deep mutational scanning.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- [Construction of the pIRES2-ZsGreen1 eukaryotic expression vector of Factor Ⅸ gene and expression in HEK-293 cells].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2016Article
- Bacterial Inner-membrane Display for Screening a Library of Antibody Fragments.Journal of visualized experiments : JoVE · 2016Article
- Making water-soluble integral membrane proteins in vivo using an amphipathic protein fusion strategy.Nature communications · 2015Article
- Repurposing a bacterial quality control mechanism to enhance enzyme production in living cells.Journal of molecular biology · 2015Article
- A method for multiplex gene synthesis employing error correction based on expression.PloS one · 2015Article
- Screening strategies to identify HSP70 modulators to treat Alzheimer's disease.Drug design, development and therapy · 2015Review
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3 authors at 2 institutions in 1 country.
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Abstract
One of the most vexing problems facing structural genomics efforts and the biotechnology enterprise in general is the inability to efficiently produce functional proteins due to poor folding and insolubility. Additionally, protein misfolding and aggregation has been linked to a number of human diseases, such as Alzheimer's. Thus, a robust cellular assay that allows for direct monitoring, manipulation, and improvement of protein folding could have a profound impact. We report the development and characterization of a genetic selection for protein folding and solubility in living bacterial cells. The basis for this assay is the observation that protein transport through the bacterial twin-arginine translocation (Tat) pathway depends on correct folding of the protein prior to transport. In this system, a test protein is expressed as a tripartite fusion between an N-terminal Tat signal peptide and a C-terminal TEM1 beta-lactamase reporter protein. We demonstrate that survival of Escherichia coli cells on selective medium expressing a Tat-targeted test protein/beta-lactamase fusion correlates with the solubility of the test protein. Using this assay, we isolated solubility-enhanced variants of the Alzheimer's Abeta42 peptide from a large combinatorial library of Abeta42 sequences, thereby confirming that our assay is a highly effective selection tool for soluble proteins. By allowing the bacterial Tat pathway to exert folding quality control on expressed target protein sequences, we have generated a powerful tool for monitoring protein folding and solubility in living cells, for molecular engineering of solubility-enhanced proteins or for the isolation of factors and/or cellular conditions that stabilize aggregation-prone proteins.
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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.