ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo

Udhayabhaskar Sathyanarayanan, Marina Musa, Peter Bou Dib, Nuno Raimundo, Ira Milosevic and Anita Krisko ()
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Udhayabhaskar Sathyanarayanan: European Neuroscience Institute (ENI) – A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society
Marina Musa: European Neuroscience Institute (ENI) – A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society
Peter Bou Dib: Universitätsmedizin Göttingen, Institut für Zellbiochemie
Nuno Raimundo: Universitätsmedizin Göttingen, Institut für Zellbiochemie
Ira Milosevic: European Neuroscience Institute (ENI) – A Joint Initiative of the University Medical Center Göttingen and the Max-Planck-Society
Anita Krisko: University Medical Center Göttingen

Nature Communications, 2020, vol. 11, issue 1, 1-17

Abstract: Abstract 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.

Date: 2020
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19104-1

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DOI: 10.1038/s41467-020-19104-1

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