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TitleThe DEAD-box Protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation.
Journal, issue, pagesPLoS Biol, Vol. 14, Issue 6, Page e1002480, Year 2016
Publish dateJun 9, 2016
AuthorsSohail Khoshnevis / Isabel Askenasy / Matthew C Johnson / Maria D Dattolo / Crystal L Young-Erdos / M Elizabeth Stroupe / Katrin Karbstein /
PubMed AbstractDEAD-box proteins are ubiquitous regulators of RNA biology. While commonly dubbed "helicases," their activities also include duplex annealing, adenosine triphosphate (ATP)-dependent RNA binding, and ...DEAD-box proteins are ubiquitous regulators of RNA biology. While commonly dubbed "helicases," their activities also include duplex annealing, adenosine triphosphate (ATP)-dependent RNA binding, and RNA-protein complex remodeling. Rok1, an essential DEAD-box protein, and its cofactor Rrp5 are required for ribosome assembly. Here, we use in vivo and in vitro biochemical analyses to demonstrate that ATP-bound Rok1, but not adenosine diphosphate (ADP)-bound Rok1, stabilizes Rrp5 binding to 40S ribosomes. Interconversion between these two forms by ATP hydrolysis is required for release of Rrp5 from pre-40S ribosomes in vivo, thereby allowing Rrp5 to carry out its role in 60S subunit assembly. Furthermore, our data also strongly suggest that the previously described accumulation of snR30 upon Rok1 inactivation arises because Rrp5 release is blocked and implicate a previously undescribed interaction between Rrp5 and the DEAD-box protein Has1 in mediating snR30 accumulation when Rrp5 release from pre-40S subunits is blocked.
External linksPLoS Biol / PubMed:27280440 / PubMed Central
MethodsEM (single particle)
Resolution30.0 Å
Structure data

EMDB-6654:
Negative stain 3DEM structure of Rrp5
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-6655:
3DEM structure of Rrp5 bound to H45-3ITS1 RNA
Method: EM (single particle) / Resolution: 30.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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