Interplay between Chaperones and Protein Disorder Promotes the Evolution of Protein Networks
Figure 6
Cost-benefit trade-off in protein network evolvability.
Complementary cellular quality control strategies promote non-conservative mutations, thus the evolvability of protein interactions. Intrinsically disordered proteins allow more non-conservative substitutions, but are subject to a more costly regulated turn-over to prevent their aggregation. While energetically expensive, molecular chaperones can promote non-conservative substitutions directly by buffering their destabilizing effect, or indirectly by stabilizing intrinsically disordered proteins. By conferring robustness to otherwise deleterious mutations, protein quality control mechanisms facilitate a higher number of non-conservative mutations, which increases the likelihood of evolving new protein interactions and functions.