Post-translational modifications (PTMs) have been extensively studied in both eukaryotes
and prokaryotes. Lysine acetylation, originally thought to be a rare occurrence in bacteria, is …

Post-translational modifications (PTM) decorate proteins to provide functional heterogeneity
to an existing proteome. The large number of known PTMs highlights the many ways that …

Post‐translational modifications of proteins are key events in cellular metabolism and
physiology regulation. Lysine acetylation is one of the best studied protein modifications in …

Posttranslational modification of a protein, either alone or in combination with other
modifications, can control properties of that protein, such as enzymatic activity, localization …

Protein lysine acetylation is a reversible and highly regulated post‐translational modification
with the well demonstrated physiological relevance in eukaryotes. Recently, its important …

Recently published work indicates that reversible Nɛ-lysine (Nɛ-Lys) acetylation of proteins
in bacteria may be as diverse, and as important for cellular function, as it has been reported …

Nε‐lysine acetylation, a reversible and highly regulated PTM, has been shown to occur in
the model Gram‐negative bacteria Escherichia coli and Salmonella enterica. Here, we …

Recent studies have revealed the physiological significance of post-translational lysine
acylations such as acetylation in the regulation of various cellular processes. Here, we …

The emerging view of Nε-lysine acetylation in eukaryotes is of a relatively abundant post-
translational modification (PTM) that has a major impact on the function, structure, stability …

Working with microbes provides opportunities to better understand fundamental cellular
processes, including some that, although discovered in eukaryotes, have their origins in …