ArticleApplied and environmental microbiology2009
Significant enhanced expression and solubility of human proteins in Escherichia coli by fusion with protein S from Myxococcus xanthus.
Article in Applied and environmental microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 29 citations in OpenAlex.
- Cooperative and divergent properties of bacterial actin isoforms inBiophysics and physicobiology · 2026Article
- Cell-permeable bone morphogenetic protein 2 facilitates bone regeneration by promoting osteogenesis.Materials today. Bio · 2024Article
- Fabrication of silica on chitin in ambient conditions using silicatein fused with a chitin-binding domain.Bioprocess and biosystems engineering · 2021Article
- Suppression of the toxicity of Bac7 (1-35), a bovine peptide antibiotic, and its production in E. coli.AMB Express · 2016Article
- An endogenous protein inhibitor, YjhX (TopAI), for topoisomerase I from Escherichia coli.Nucleic acids research · 2015Article
- Semi-synthesis of labeled proteins for spectroscopic applications.Molecules (Basel, Switzerland) · 2013Review
- Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression.Biochemistry · 2012Article
- Segmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubility.Journal of biomolecular NMR · 2012Article
- Noncognate Mycobacterium tuberculosis toxin-antitoxins can physically and functionally interact.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Protein S is a major spore coat protein of Myxococcus xanthus, consisting of two homologous domains, the N-terminal domain (NTD) and the C-terminal domain, both of which contain a Ca(2+)-binding site. Protein S tightly binds to myxospores in a Ca(2+)-dependent manner. Here, we constructed a novel expression vector, pCold-PST, encoding two tandem repeat NTDs (PrS2). By using this vector, a number of human proteins that were expressed at low levels or in insoluble forms by a pET vector were expressed not only at high levels but also in soluble forms. We also demonstrated that an Escherichia coli protein tagged with PrS2 fully retained its function, indicating that it is folded independently from the tag. This technology not only allows simple, one-step protein purification using myxospores, but can also be used for the identification of proteins interacting with a protein of interest and will prove immensely useful for structural studies of proteins which are difficult to produce or are insoluble.
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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.