ArticleProtein science : a publication of the Protein Society2004
An efficient system for high-level expression and easy purification of authentic recombinant proteins.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.
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152 citing papers in PubMed.
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- The ancestral ESCRT protein TOM1L2 selects ubiquitinated cargoes for retrieval from cilia.Developmental cell · 2023Article
- Cryo-EM structures of human SPCA1a reveal the mechanism of CaScience advances · 2023Article
92 more citing papers are in PubMed but not listed here.
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5 authors.
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Abstract
Expression of recombinant proteins as fusions to the eukaryotic protein ubiquitin has been found to significantly increase the yield of unstable or poorly expressed proteins. The benefit of this technique is further enhanced by the availability of naturally occurring deubiquitylating enzymes, which remove ubiquitin from the fusion product. However, the versatility of the system has been constrained due to the lack of a robust, easily purified deubiquitylating enzyme. Here we report the development of an efficient expression system, utilizing the ubiquitin fusion technique, which allows convenient high yield and easy purification of authentic protein. An Escherichia coli vector (pHUE) was constructed for the expression of proteins as histidine-tagged ubiquitin fusions, and a histidine-tagged deubiquitylating enzyme to cleave these fusions was expressed and purified. The expression system was tested using several proteins varying in size and complexity. These results indicate that this procedure will be suitable for the expression and rapid purification of a broad range of proteins and peptides, and should be amenable to high-throughput applications.
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