The hibernating 100S complex is a target of ribosome-recycling factor and elongation factor G in Staphylococcus aureus.

ABSTRACT: The formation of translationally inactive 70S dimers (called 100S ribosomes) by hibernation-promoting factor is a widespread survival strategy among bacteria. Ribosome dimerization is thought to be reversible, with the dissociation of the 100S complexes enabling ribosome recycling for participation in new rounds of translation. The precise pathway of 100S ribosome recycling has been unclear. We previously found that the heat-shock GTPase HflX in the human pathogen Staphylococcus aureus is a minor disassembly factor. Cells lacking hflX do not accumulate 100S ribosomes unless they are subjected to heat exposure, suggesting the existence of an alternative pathway during nonstressed conditions. Here, we provide biochemical and genetic evidence that two essential translation facto

SUBMITTER: Basu A 

PROVIDER: S-EPMC7196661 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature