A Novel Method for Assessing the Chaperone Activity of Proteins.

TitleA Novel Method for Assessing the Chaperone Activity of Proteins.
Publication TypeJournal Article
Year of Publication2016
AuthorsHristozova, N., P. Tompa, and D. Kovacs
JournalPLoS One
Date Published2016
KeywordsAlcohol Dehydrogenase, Citrate (si)-Synthase, L-Lactate Dehydrogenase, Luciferases, Molecular Chaperones, Protein Array Analysis, Protein Binding, Protein Folding, Proteins

Protein chaperones are molecular machines which function both during homeostasis and stress conditions in all living organisms. Depending on their specific function, molecular chaperones are involved in a plethora of cellular processes by playing key roles in nascent protein chain folding, transport and quality control. Among stress protein families-molecules expressed during adverse conditions, infection, and diseases-chaperones are highly abundant. Their molecular functions range from stabilizing stress-susceptible molecules and membranes to assisting the refolding of stress-damaged proteins, thereby acting as protective barriers against cellular damage. Here we propose a novel technique to test and measure the capability for protective activity of known and putative chaperones in a semi-high throughput manner on a plate reader. The current state of the art does not allow the in vitro measurements of chaperone activity in a highly parallel manner with high accuracy or high reproducibility, thus we believe that the method we report will be of significant benefit in this direction. The use of this method may lead to a considerable increase in the number of experimentally verified proteins with such functions, and may also allow the dissection of their molecular mechanism for a better understanding of their function.

Alternate JournalPLoS ONE
PubMed ID27564234
PubMed Central IDPMC5001627
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