Protein synthesis during cellular quiescence is inhibited by phosphorylation of a translational elongation factor.

ABSTRACT: In nature, most organisms experience conditions that are suboptimal for growth. To survive, cells must fine-tune energy-demanding metabolic processes in response to nutrient availability. Here, we describe a novel mechanism by which protein synthesis in starved cells is down-regulated by phosphorylation of the universally conserved elongation factor Tu (EF-Tu). Phosphorylation impairs the essential GTPase activity of EF-Tu, thereby preventing its release from the ribosome. As a consequence, phosphorylated EF-Tu has a dominant-negative effect in elongation, resulting in the overall inhibition of protein synthesis. Importantly, this mechanism allows a quick and robust regulation of one of the most abundant cellular proteins. Given that the threonine that serves as the primary site of phospho

SUBMITTER: Pereira SF 

PROVIDER: S-EPMC4485140 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature