Reversible protein phosphorylation on serine, threonine, and tyrosine (Ser/Thr/Tyr) residues
plays a critical role in regulation of vital processes in the cell. Despite of considerable …

Increasing evidence shows that protein phosphorylation on serine (Ser), threonine (Thr),
and tyrosine (Tyr) residues is one of the major post-translational modifications in the …

Mycoplasma pneumoniae belongs to the Mollicutes, the group of organisms with the
smallest genomes that are capable of host-independent life. These bacteria show little …

While phosphotyrosine modification is an established regulatory mechanism in eukaryotes,
it is less well characterized in bacteria due to low prevalence. To gain insight into the extent …

High accuracy mass spectrometry has proven to be a powerful technology for the large scale
identification of serine/threonine/tyrosine phosphorylation in the living cell. However, despite …

Quantitative proteomics has become an indispensable analytical tool for microbial research.
Modern microbial proteomics covers a wide range of topics in basic and applied research …

Protein investment costs are considered a major driver for the choice of alternative metabolic
strategies. We tested this premise in L actococcus lactis, a bacterium that exhibits a distinct …

Bacteria can detect, transmit, and react to signals from the outside world by using two-
component systems (TCS) and serine-threonine kinases and phosphatases. Streptococcus …

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 …

In prokaryotes and eukaryotes, phosphotransfer represents a common mechanism to
regulate cellular functions. Recent work revealed that modulation of cellular processes by …