Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors

ABSTRACT: Ribosomal action is facilitated by the orchestrated work of trans-acting factors and ribosomal elements, which are subject to regulatory events, often involving phosphorylation. One such element is the ribosomal P-stalk, which plays a dual function: it activates translational GTPases, which support basic ribosomal functions, and interacts with the Gcn2 kinase, linking the ribosomes to the ISR pathway. We show that P-stalk proteins, which form a pentamer, exist in the cell exclusively in a phosphorylated state at five C-terminal domains (CTDs), ensuring optimal translation (speed and accuracy) and may play a role in the timely regulation of the Gcn2-dependent stress response. Phosphorylation of the CTD induces a structural transition from a collapsed to a coil-like structure, and the CTD ga

SUBMITTER: Dr. Kamil Filipek 

PROVIDER: S-SCDT-10_1038-S44319-024-00297-1 | biostudies-other |

REPOSITORIES: biostudies-other