Structures and dynamics of hibernating ribosomes from <i>Staphylococcus aureus</i> mediated by intermolecular interactions of HPF.

ABSTRACT: In bacteria, ribosomal hibernation shuts down translation as a response to stress, through reversible binding of stress-induced proteins to ribosomes. This process typically involves the formation of 100S ribosome dimers. Here, we present the structures of hibernating ribosomes from human pathogen Staphylococcus aureus containing a long variant of the hibernation-promoting factor (SaHPF) that we solved using cryo-electron microscopy. Our reconstructions reveal that the N-terminal domain (NTD) of SaHPF binds to the 30S subunit as observed for shorter variants of HPF in other species. The C-terminal domain (CTD) of SaHPF protrudes out of each ribosome in order to mediate dimerization. Using NMR, we characterized the interactions at the CTD-dimer interface. Secondary interactions are p

SUBMITTER: Khusainov I 

PROVIDER: S-EPMC5510003 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature