We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Hsp70-associated chaperones have a critical role in buffering protein production costs.
- Authors
Farkas, Zoltán; Kalapis, Dorottya; Bódi, Zoltán; Szamecz, Béla; Daraba, Andreea; Almási, Karola; Kovács, Károly; Boross, Gábor; Pál, Ferenc; Horváth, Péter; Balassa, Tamás; Molnár, Csaba; Pettkó-Szandtner, Aladar; Klement, Éva; Rutkai, Edit; Szvetnik, Attila; Papp, Balázs; Pál, Csaba
- Abstract
Proteins are necessary for cellular growth. Concurrently, however, protein production has high energetic demands associated with transcription and translation. Here, we propose that activity of molecular chaperones shape protein burden, that is the fitness costs associated with expression of unneeded proteins. To test this hypothesis, we performed a genome-wide genetic interaction screen in baker's yeast. Impairment of transcription, translation, and protein folding rendered cells hypersensitive to protein burden. Specifically, deletion of specific regulators of the Hsp70-associated chaperone network increased protein burden. In agreement with expectation, temperature stress, increased mistranslation and a chemical misfolding agent all substantially enhanced protein burden. Finally, unneeded protein perturbed interactions between key components of the Hsp70-Hsp90 network involved in folding of native proteins. We conclude that specific chaperones contribute to protein burden. Our work indicates that by minimizing the damaging impact of gratuitous protein overproduction, chaperones enable tolerance to massive changes in genomic expression.
- Subjects
HSP70 heat-shock proteins; MOLECULAR chaperones; PROTEIN expression; GENE expression; GENETIC overexpression
- Publication
eLife, 2018, p1
- ISSN
2050-084X
- Publication type
Article
- DOI
10.7554/eLife.29845