phosphorylation, acetylation, ubiquitination, methylation, etc.—that are added to molecular chaperones to modulate their activity.
Because post-translational modifications are marks that can be added and removed rapidly, they provide an efficient mechanism to explain the plasticity observed in proteome organization during cell growth and development.
In some cases phosphorylation may disrupt the interaction with a co-chaperone protein thus negatively affecting its activity.
[2][10] Certain pathogenic bacteria may manipulate host chaperone phosphorylation through bacterial effectors to promote their survival.
HoPBF1, a family of bacterial effector protein kinases, phosphorylates HSP90 at Serine 99 to dampen immunity.