Post-translational modifications act as rheostats of protein activity. Many them reflect environmental variations and allow the cell to give an adapted response these changes. In this cover article #Ref, Céline Schulz collaborators provide in-depth overview still underrated role nutrient-dependent post-translational modification O-GlcNAcylation in regulation metabolism lipids, a very heterogeno...

Amide peptide backbone methylation is a characteristic post-translational modification found in family of ribosomally synthesized and post-translationally modified natural products (RiPPs) called borosins. Previously, we bioinformatically identified >1500...

Many proteins, particularly those derived from eukaryotic sources, undergo covalent modification either during their ribosomal synthesis or (more usually) after synthesis is complete, giving rise to the concept of co-translational and post-translational modification. While the stage during protein synthesis/maturation at which the coor post-translational modification occurs obviously differs, b...

PII proteins are pivotal players in the control of nitrogen metabolism in bacteria and archaea, and are also found in the plastids of plants. PII proteins control the activities of a diverse range of enzymes, transcription factors and membrane transport proteins, and their regulatory effect is achieved by direct interaction with their target. Many, but by no means all, PII proteins are subject ...

Aggregation of Cu,Zn superoxide dismutase (SOD1) is implicated in amyotrophic lateral sclerosis. Glutathionylation and phosphorylation of SOD1 is omnipresent in the human body, even in healthy individuals, and has been shown to increase SOD1 dimer dissociation, which is the first step on the pathway toward SOD1 aggregation. We found that post-translational modification of SOD1, especially gluta...