Dom34-Hbs1 mediated dissociation of inactive 80S ribosomes promotes restart of translation after stress

Antonia M.G. Van Den Elzen, Anthony Schuller, Rachel Green, Bertrand Séraphin

Research output: Contribution to journalArticlepeer-review

45 Scopus citations


Following translation termination, ribosomal subunits dissociate to become available for subsequent rounds of protein synthesis. In many translation-inhibiting stress conditions, e.g. glucose starvation in yeast, free ribosomal subunits reassociate to form a large pool of non-translating 80S ribosomes stabilized by the 'clamping' Stm1 factor. The subunits of these inactive ribosomes need to be mobilized for translation restart upon stress relief. The Dom34-Hbs1 complex, together with the Rli1 NTPase (also known as ABCE1), have been shown to split ribosomes stuck on mRNAs in the context of RNA quality control mechanisms. Here, using in vitro and in vivo methods, we report a new role for the Dom34-Hbs1 complex and Rli1 in dissociating inactive ribosomes, thereby facilitating translation restart in yeast recovering from glucose starvation stress. Interestingly, we found that this new role is not restricted to stress conditions, indicating that in growing yeast there is a dynamic pool of inactive ribosomes that needs to be split by Dom34-Hbs1 and Rli1 to participate in protein synthesis. We propose that this provides a new level of translation regulation.

Original languageEnglish (US)
Pages (from-to)265-276
Number of pages12
JournalEMBO Journal
Issue number3
StatePublished - Feb 3 2014


  • Glucose-starvation
  • Initiation
  • Ribosome recycling
  • Rli1
  • Stm1
  • T.
  • Translation

ASJC Scopus subject areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • General Immunology and Microbiology


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