Survival of the drowsiest: the hibernating 100S ribosome in bacterial stress management

David W. Gohara, Mee-Ngan Frances Yap*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

31 Scopus citations

Abstract

In response to nutrient deprivation and environmental insults, bacteria conjoin two copies of non-translating 70S ribosomes that form the translationally inactive 100S dimer. This widespread phenomenon is believed to prevent ribosome turnover and serves as a reservoir that, when conditions become favorable, allows the hibernating ribosomes to be disassembled and recycled for translation. New structural studies have revealed two distinct mechanisms for dimerizing 70S ribosomes, but the molecular basis of the disassembly process is still in its infancy. Many details regarding the sequence of dimerization-dissociation events with respect to the binding and departure of the hibernation factor and its antagonizing disassembly factor remain unclear.

Original languageEnglish (US)
Pages (from-to)753-760
Number of pages8
JournalCurrent Genetics
Volume64
Issue number4
DOIs
StatePublished - Aug 1 2018

Keywords

  • HPF
  • HflX
  • Ribosome
  • Stress response
  • Translation

ASJC Scopus subject areas

  • Genetics

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