Disassembly of the Staphylococcus aureus hibernating 100S ribosome by an evolutionarily conserved GTPase.

ABSTRACT: The bacterial hibernating 100S ribosome is a poorly understood form of the dimeric 70S particle that has been linked to pathogenesis, translational repression, starvation responses, and ribosome turnover. In the opportunistic pathogen Staphylococcus aureus and most other bacteria, hibernation-promoting factor (HPF) homodimerizes the 70S ribosomes to form a translationally silent 100S complex. Conversely, the 100S ribosomes dissociate into subunits and are presumably recycled for new rounds of translation. The regulation and disassembly of the 100S ribosome are largely unknown because the temporal abundance of the 100S ribosome varies considerably among different bacterial phyla. Here, we identify a universally conserved GTPase (HflX) as a bona fide dissociation factor of the S. a

SUBMITTER: Basu A 

PROVIDER: S-EPMC5625922 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature