The bacterial phosphoenolpyruvate (PEP): carbohydrate phosphotransferase system (PTS)
carries out both catalytic and regulatory functions. It catalyzes the transport and …

The reversible phosphorylation of proteins is accomplished by opposing activities of kinases
and phosphatases. Relatively few protein serine/threonine phosphatases (PSPs) control the …

Genomic studies have revealed the presence of Ser/Thr kinases and phosphatases in many
bacterial species, although their physiological roles have largely been unclear. Here we …

Post-translational modification of proteins by lysine acetylation plays important regulatory
roles in living cells. The budding yeast Saccharomyces cerevisiae is a widely used …

Protein phosphorylation is a key posttranslational modification, which reversibly regulates
almost all processes in the living cell. Deregulated signaling is a hallmark of cancer and …

The post-translational modification (PTM) of proteins plays a critical role in the regulation of
a broad range of cellular processes in eukaryotes. Yet their role in governing similar systems …

Posttranslational modification of proteins by acetylation and phosphorylation regulates most
cellular processes in living organisms. Surprisingly, the evolutionary conservation of …

The Mycobacterium tuberculosis genome encodes 11 serine/threonine protein kinases
(STPKs) that are structurally related to eukaryotic kinases. To gain insight into the role of …

Protein phosphorylation appears to be a universal mechanism of protein regulation.
Genomics has provided the means to compile inventories of protein phosphatases across a …

The important human pathogen Pseudomonas aeruginosa has been linked to numerous
biofilm-related chronic infections. Here, we demonstrate that biofilm formation following the …