Background: Molecular chaperones assist proteins to gain their three-dimensional conformation or triage damaged proteins for degradation. Results: The chaperone Aha1 prevents aggregation of stressed denatured proteins and favors their ubiquitination. Conclusion: Aha1 may save the protein folding machinery from overload by misfolded proteins. Significance: This new function of Aha1 may be crucial to avoid harm to the cell.
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