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- Title
Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein.
- Authors
Wigley, W. Christian; Stidham, Rhesa D.; Smith, Nathan M.; Hunt, John F.; Thomas, Philip J.
- Abstract
Protein misfolding is the basis of a number of human diseases and presents an obstacle to the production of soluble recombinant proteins. We present a general method to assess the solubility and folding of proteinsin vivo. The basis of this assay is structural complementation between the α- and ω-fragments of β-galactosidase (β-gal). Fusions of the α-fragment to the C terminus of target proteins with widely varying in vivo folding yield and/or solubility levels, including the Alzheimer's amyloid β (Aβ) peptide and a non-amyloidogenic mutant thereof, reveal an unambiguous correlation between β-gal activity and the solubility/folding of the target. Thus, structural complementation provides a means of monitoring protein solubility/misfolding in vivo, and should find utility in the screening for compounds that influence the pathological consequences of these processes.
- Subjects
PROTEIN folding; RECOMBINANT proteins; GENETIC markers
- Publication
Nature Biotechnology, 2001, Vol 19, Issue 2, p131
- ISSN
1087-0156
- Publication type
Article
- DOI
10.1038/84389