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An efficient system for high‐level expression and easy purification of authentic recombinant proteins
Open accessAbstract
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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Cited by
Dodds, P. N., Lawrence, G. J., Catanzariti, A.-M., Teh, T., Wang, C.-I. A., Ayliffe, M. A., Kobe, B., & Ellis, J. G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0602577103 · Cited by 787
Self-citationSUMO fusion technology for difficult-to-express proteins
Butt, T. R., Edavettal, S. C., Hall, J. P., & Mattern, M. R. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2005.03.016 · Cited by 517
Efficient backbone cyclization of linear peptides by a recombinant asparaginyl endopeptidase
Harris, K. S., Durek, T., Kaas, Q., Poth, A. G., Gilding, E. K., Conlan, B. F., Saska, I., Daly, N. L., van der Weerden, N. L., Craik, D. J., et al. (2015) · Nature Communications · doi:10.1038/ncomms10199 · Cited by 257
Control of angiogenesis by AIBP-mediated cholesterol efflux
Fang, L., Choi, S.-H., Baek, J. S., Liu, C., Almazan, F., Ulrich, F., Wiesner, P., Taleb, A., Deer, E., Pattison, J., et al. (2013) · Nature · doi:10.1038/nature12166 · Cited by 192
Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase
Mueller-Cajar, O., Stotz, M., Wendler, P., Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10568 · Cited by 190
Metadata
- Authors
- Catanzariti, A., Soboleva, T. A., Jans, D. A., Board, P. G., & Baker, R. T.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2004-05
- Volume
- 13
- Issue
- 5
- Pages
- 1331-1339
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2105624689
- Cited by
- 298
- References
- 0
- FWCI
- 3.61
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Catanzariti, A., Soboleva, T. A., Jans, D. A., Board, P. G., & Baker, R. T. (2004). An efficient system for high‐level expression and easy purification of authentic recombinant proteins. Protein Science. https://doi.org/10.1110/ps.04618904
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