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Enhanced Expression and Purification of Membrane Proteins by SUMO Fusion in Escherichia coli
Journal article   Open access   Peer reviewed

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

Xun Zuo, Shuisen Li, John Hall, Michael R. Mattern, Hiep Tran, Joshua Shoo, Robin Tan, Susan R. Weiss and Tauseef R. Butt
Journal of structural and functional genomics, v 6(2)
01 Jan 2005
DOI: https://doi.org/10.1007/s10969-005-2664-4
PMID: 16211506
url
https://doi.org/10.1007/s10969-005-2664-4View
Published, Version of Record (VoR)Maybe Open Access (Publisher Bronze),  Open

Abstract

5-lipoxygenase activating protein (FLAP) membrane protein expression Nickel affinity purification SARS-CoV membrane protein SUMO fusion
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 .

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