Functional definition of NrtR and the discovery of its acetylation represents a first paradigm for linking protein acetylation to bacterial central NAD⁺ metabolism.

Chromatin structure is altered following DNA replication stress through the activity of protein kinase C signalling which leads to functionally coupled histone H3 phosphorylation and acetylation events.

Biochemical reconstitution of deadenylation and analysis of binding kinetics reveals how RNA-binding proteins select their mRNA targets.

Acetylation of the circadian transcription factor BMAL1 by the acetyltransferase TIP60 is crucial for recruitment of the pause release factors to clock gene promoters and productive elongation of these genes.

The cryo-EM structure of the human N-terminal acetyltransferase NatB bound to a cognate N-terminal alpha-synuclein peptide reveals the molecular determinants of NatB-specific protein acetylation.

LARP4 protects mRNAs against deadenylation over a wide range of poly(A) lengths but with most apparent functional impact on short lengths known to sensitize PABP binding and mRNA stability.

FGF signalling is responsible for priming the developmental enhancer ZRS across the distal limb mesenchyme during development, allowing ETS factors to modulate its activity through balancing histone acetylation.

The acetylation of histones at specific sites close to DNA can regulate transcription.

A versatile acetylation-methylation switch at lysine 31 on the lateral surface of histone H4 contributes to chromatin structure in apicomplexan parasites.

Mass spectroscopy, molecular modeling and/or molecular dynamics simulations reveal how acetylation regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation.