NDLI: Enhanced Expression and Purification of Membrane Proteins by SUMO Fusion in Escherichia coli

Content Provider	Springer Nature Link
Author	Zuo, Xun Li, Shuisen Hall, John Mattern, Michael R. Tran, Hiep Shoo, Joshua Tan, Robin Weiss, Susan R. Butt, Tauseef R.
Copyright Year	2005
Abstract	Severe acute respiratory syndrome coronavirus (SARS-CoV) membrane protein and 5-lipoxygenase-activating protein (FLAP) are among a large number of membrane proteins that are poorly expressed when traditional expression systems and methods are employed. Therefore to efficiently express difficult membrane proteins, molecular biologists will have to develop novel or innovative expression systems. To this end, we have expressed the SARS-CoV M and FLAP proteins in Escherichia coli by utilizing a novel gene fusion expression system that takes advantage of the natural chaperoning properties of the SUMO (small ubiquitin-related modifier) tag. These chaperoning properties facilitate proper protein folding, which enhances the solubility and biological activity of the purified protein. In addition to these advantages, we found that SUMO Protease 1, can cleave the SUMO fusion high specificity to generate native protein. Herein, we demonstrate that the expression of FLAP and SARS-CoV membrane proteins are greatly enhanced by SUMO fusions in E. coli.
Starting Page	103
Ending Page	111
Page Count	9
File Format	PDF
ISSN	1345711X
Journal	Journal of Structural and Functional Genomics
Volume Number	6
Issue Number	2-3
e-ISSN	15700267
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	2005-01-01
Publisher Place	Dordrecht
Access Restriction	Subscribed
Subject Keyword	5-lipoxygenase activating protein (FLAP) membrane protein expression Nickel affinity purification SARS-CoV membrane protein SUMO fusion Human Genetics Bioinformatics Microbial Genetics and Genomics Plant Genetics & Genomics Animal Genetics and Genomics Biochemistry
Content Type	Text
Resource Type	Article
Subject	Genetics Structural Biology Biochemistry

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