In vitro characterization of the yeast DEAH/RHA RNA helicase Dhr1.

ABSTRACT: In eukaryotic ribosome biogenesis, the small subunit (SSU) processome is a metastable intermediate in the assembly of the small (40S) subunit. In the SSU processome, the ribosomal RNA domains are splayed open by the intervention of assembly factors as well as U3 snoRNA. A critical step during the transition from the SSU processome to the nearly mature pre-40S particle is the removal of the U3 snoRNA to allow the formation of the central pseudoknot, a universally conserved structure which connects all domains of the subunit and contributes to its dynamic nature during translation. We previously identified the DEAH/RHA RNA helicase Dhr1 as the enzyme responsible for displacing the U3 snoRNA and the SSU processome factor Utp14 as an activator of Dhr1. Here, we have utilized biochemical and ye

SUBMITTER: Lin R 

PROVIDER: S-EPMC11994318 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature