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Signs of proteostasis failure often entwine with those of metabolic stress at the cellular level. Here, we study protein sequestration during glucose deprivation-induced ATP decline in Saccharomyces cerevisiae. Using live-cell imaging, we find that sequestration of misfolded proteins and nascent polypeptides into two distinct compartments, stress granules, and Q-bodies, is triggered by the exhaustion of ATP. Both compartments readily dissolve in a PKA-dependent manner within minutes of glucose reintroduction and ATP level restoration. We identify the ATP hydrolase activity of Hsp104 disaggregase as the critical ATP-consuming process determining compartments abundance and size, even in optimal conditions. Sequestration of proteins into distinct compartments during acute metabolic stress and their retrieval during the recovery phase provide a competitive fitness advantage, likely promoting cell survival during stress.

Original publication

DOI

10.1038/s41467-020-19104-1

Type

Journal article

Journal

Nature communications

Publication Date

16/10/2020

Volume

11

Addresses

European Neuroscience Institute (ENI) - A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society, Göttingen, Germany.

Keywords

Saccharomyces cerevisiae, Glucose, Saccharomyces cerevisiae Proteins, Heat-Shock Proteins, Adenosine Triphosphate, Hydrolysis, Solubility, Protein Aggregates