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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Al-Samarrai, T.H. et al.

Al-Samarrai, Kirk, Jones, Harvey, Sun,

Expression in Escherichia coli and in vitro refolding of the plant transcription factor Arabidopsis thaliana RGL3.

Recombinant Arabidopsis thaliana (At) RGL-3, using two vectors pMAL-c2 and pET 21, was expressed as inclusion bodies in Escherichia coli under a range of temperature conditions. Only low levels (8-12% of total protein) of soluble protein were produced. The "soluble" fraction was shown by native PAGE to exist as soluble aggregates of RGL-3. A method was developed, consisting of induction of expression at various temperatures that yielded high levels of refoldable inclusion bodies using the pET vector. (At) RGL-3, as inclusion bodies, was solubilized in 8M urea and refolding was initiated by 20-fold direct dilution of denaturant. Under optimal conditions, 87% of the denatured protein of inclusion bodies was successfully re-natured. Refolding was monitored by "native" PAGE. Refolded RGL-3 was shown to be present as monomers and dimers. Attempts to further purify His-tagged RGL-3 using Ni/NTA chromatography resulted in the formation of higher polymers.[1]

References

Expression in Escherichia coli and in vitro refolding of the plant transcription factor Arabidopsis thaliana RGL3. Al-Samarrai, T.H., Kirk, C.A., Jones, W.T., Harvey, D., Sun, X. Protein Expr. Purif. (2007) [Pubmed]

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