Evidence suggesting that eukaryotes and archaea use reversible N ε-lysine (N ε-Lys)
acetylation to modulate gene expression has been reported, but evidence for bacterial use …

N𝜀-lysine acetylation is an abundant and important Post-translational modification in
bacteria. We used the bacterial two-hybrid system to screen the genome library of the …

ABSTRACT Nε-lysine acetylation was recently discovered on many bacterial proteins that
function in diverse cellular processes. Thus, many questions remain unanswered. For …

ABSTRACT N ε-Lysine acetylation has been recognized as a ubiquitous regulatory
posttranslational modification that influences a variety of important biological processes in …

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 …

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

Posttranslational modifications, such as N ε-lysine acetylation, regulate protein function. N ε-
lysine acetylation can occur either nonenzymatically or enzymatically. The nonenzymatic …

CysB is a LysR‐type transcriptional regulator (LTTR) controlling the expression of numerous
genes involved in bacterial sulphur assimilation via cysteine biosynthesis. Our previous …

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 is an abundant and dynamic regulatory posttranslational modification
that remains poorly characterized in bacteria. In bacteria, hundreds of proteins are known to …