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

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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
    Mediterranean Institute for Life Sciences)

  • 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
    University of Oxford)

  • Anita Krisko

    (University Medical Center Göttingen)

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.

Suggested Citation

  • Udhayabhaskar Sathyanarayanan & Marina Musa & Peter Bou Dib & Nuno Raimundo & Ira Milosevic & Anita Krisko, 2020. "ATP hydrolysis by yeast Hsp104 determines protein aggregate dissolution and size in vivo," Nature Communications, Nature, vol. 11(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19104-1
    DOI: 10.1038/s41467-020-19104-1
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    Cited by:

    1. Arthur Fischbach & Angela Johns & Kara L. Schneider & Xinxin Hao & Peter Tessarz & Thomas Nyström, 2023. "Artificial Hsp104-mediated systems for re-localizing protein aggregates," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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