Impact of phosphoproteomics on studies of bacterial physiology
Résumé
Protein phosphorylation on serine, threonine and tyrosine is recognized as a major tool of signal transduction in bacteria. However, progress in the field has been hampered by the lack of global and site-specific data on bacterial phosphoproteomes. Recent advances in mass spectrometrybased proteomics have encouraged bacteriologists to start using powerful gel-free approaches for global detection of phosphorylated proteins. These studies have generated large data sets of proteins phosphorylated on serine, threonine and tyrosine, with identified phosphorylation sites which represent an excellent starting point for in-depth physiological characterization of kinases and their substrates. The list of phosphorylated proteins inspired a number of physiological studies in which the identity of the phosphorylation site facilitated the elucidation of molecular mechanisms of signaling and regulation. Bacterial phosphoproteomics also provided interesting insights into the evolutionary aspects of protein phosphorylation. The field is rapidly embracing quantitative mass spectrometry strategies, comparing phosphoproteome dynamics in changing conditions and aiming to reconstruct the entire regulatory networks by linking kinases to their physiological substrates.
Mots clés
protein phosphorylation
protein kinase
signal transduction
mass spectrometry
bacterial physiology
PROTEIN-TYROSINE KINASE
CARBON CATABOLITE REPRESSION
BACILLUS-SUBTILIS
ESCHERICHIA-COLI
MYCOBACTERIUM-TUBERCULOSIS
PHOSPHOTRANSFERASE SYSTEM
SER/THR/TYR PHOSPHOPROTEOME
PHOSPHORYLATED PROTEINS
MASS-SPECTROMETRY
IN-VIVO