Gene expression response to misfolded protein as a screen for soluble recombinant protein

Authors: Lesley, Scott A.; Graziano, Jim; Cho, Charles Y.; Knuth, Mark W.

Source: Protein Engineering, Volume 15, Number 2, February 2002 , pp. 153-160(8)

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Abstract:

Proper protein folding is key to producing recombinant proteins for structure determination. We have examined the effect of misfolded recombinant protein on gene expression in Escherichia coli. Comparison of expression patterns indicates a unique set of genes responding to translational misfolding. The response is in part analogous to heat shock and suggests a translational component to the regulation. We have further utilized the expression information to generate reporters responsive to protein misfolding. These reporters were used to identify properly folded recombinant proteins and to create soluble domains of insoluble proteins for structural studies.

Keywords: protein chaperone; protein folding; recombinant gene expression; solubility assay

Document Type: Research article

Affiliations: 1: Genomics Institute of the Novartis Research Foundation, 3115 Merryfield Row, San Diego, CA 92121

Publication date: 2002-02-01