期刊
NATURE BIOTECHNOLOGY
卷 19, 期 2, 页码 131-136出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/84389
关键词
aggregation; folding; solubility; complementation; protein-folding diseases
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 proteins in vivo. The basis of this assay is structural complementation between the alpha- and omega -fragments of beta -galactosidase (beta -gal). Fusions of the alpha -fragment to the C terminus of target proteins with widely varying in vivo folding yield and/or solubility levels, including the Alzheimer's amyloid beta (A beta) peptide and a non-amyloidogenic mutant thereof, reveal an unambiguous correlation between beta -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.
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