Abstract:
: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.
journal_name
PLoS Bioljournal_title
PLoS biologyauthors
Khoshnevis S,Askenasy I,Johnson MC,Dattolo MD,Young-Erdos CL,Stroupe ME,Karbstein Kdoi
10.1371/journal.pbio.1002480subject
Has Abstractpub_date
2016-06-09 00:00:00pages
e1002480issue
6eissn
1544-9173issn
1545-7885pii
PBIOLOGY-D-16-00944journal_volume
14pub_type
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