The intracellular space is characterized by macromolecular crowding, featuring cytosolic macromolecules at concentrations ranging from 300 to 400 g/L [1]. Because of that, polypeptides face the risk of nonspecific interactions and aggregation, not only during synthesis but also when subjected to stress-induced unfolding; aggregation of essential proteins may ultimately lead to the loss of cellular functions critical for growth and survival. Furthermore, protein aggregates can have cytotoxic effects by binding to and disrupting functional proteins [2]. In humans, protein aggregation is associated with cellular degeneration in many age-related diseases (such as Alzheimer’s and Parkinson’s diseases, among others) [3]. Therefore, controlling protein quality and maintaining proteome homeostasis are critical for cellular survival. To achieve this, living cells rely on a network of molecular chaperones that play key roles in processes such as de novo folding, refolding or proteolytic degradation of stress-denatured proteins, oligomeric assembly, and intracellular protein trafficking 4, 5, 6, 7.