A direct nuclear magnetic resonance method to investigate lysine acetylation of intrinsically disordered proteins.

ABSTRACT: Intrinsically disordered proteins are frequent targets for functional regulation through post-translational modification due to their high accessibility to modifying enzymes and the strong influence of changes in primary structure on their chemical properties. While lysine N_ε-acetylation was first observed as a common modification of histone tails, proteomic data suggest that lysine acetylation is ubiquitous among both nuclear and cytosolic proteins. However, compared with our biophysical understanding of the other common post-translational modifications, mechanistic studies to document how lysine N_ε-acetyl marks are placed, utilized to transduce signals, and eliminated when signals need to be turned off, have not kept pace with proteomic discoveries. Herein we report

SUBMITTER: Fraser OA 

PROVIDER: S-EPMC9853081 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature