Stably enhanced histone acetylation has long been regarded as a condition of
transcriptionally active genes. Recent papers suggest a more dynamic model, with rapid …

Histones undergo several different post-translational modifications that control a variety of
physiological processes. These covalent modifications show substantial cross-regulation …

Acetylation of the ε-amino group of lysine (Lys) is a reversible posttranslational modification
recently discovered to be widespread, occurring on proteins outside the nucleus, in most …

Protein activity and turnover is tightly and dynamically regulated in living cells. Whereas the
three-dimensional protein structure is predominantly determined by the amino acid …

Mass spectrometry (MS) is a powerful tool to analyze complex mixtures of proteins in a high‐
throughput fashion. Proteome analysis has already become a routine task in biomedical …

The biological significance of recently described modifiable residues in the globular core of
the bovine nucleosome remains elusive. We have mapped these modification sites onto the …

The lysine acetylation of proteins is a reversible post-translational modification that plays a
critical regulatory role in both eukaryotes and prokaryotes. Mycobacterium tuberculosis is a …

Lysine acetylation (LysAc), a form of reversible protein posttranslational modification
previously known only for histone regulation in plants, is shown to be widespread in …

Epigenetic gene silencing in eukaryotes is regulated in part by lysine methylation of the core
histone proteins. While histone lysine methylation is known to control gene expression …

Methylation is a post-translational modification that can affect numerous features of proteins,
notably cellular localization, turnover, activity, and molecular interactions. Recent genome …