Genetic selection designed to stabilize proteins uncovers a chaperone called Spy

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DOIResolve DOI: http://doi.org/10.1038/nsmb.2016
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TypeArticle
Journal titleNature Structural & Molecular Biology
Volume18
Issue3
Pages262270; # of pages: 9
AbstractTo optimize the in vivo folding of proteins, we linked protein stability to antibiotic resistance, thereby forcing bacteria to effectively fold and stabilize proteins. When we challenged Escherichia coli to stabilize a very unstable periplasmic protein, it massively overproduced a periplasmic protein called Spy, which increases the steady-state levels of a set of unstable protein mutants up to 700-fold. In vitro studies demonstrate that the Spy protein is an effective ATP-independent chaperone that suppresses protein aggregation and aids protein refolding. Our strategy opens up new routes for chaperone discovery and the custom tailoring of the in vivo folding environment. Spy forms thin, apparently flexible cradle-shaped dimers. The structure of Spy is unlike that of any previously solved chaperone, making it the prototypical member of a new class of small chaperones that facilitate protein refolding in the absence of energy cofactors.
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedYes
NRC number53151
NPARC number18397759
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Record identifierfbff2b26-34a3-4a02-8422-b658c2ebf8d8
Record created2012-03-06
Record modified2016-05-09
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