Summary information and primary citation

PDB-id
7r7c; SNAP-derived features in text and JSON formats; DNAproDB
Class
ribosome
Method
cryo-EM (3.71 Å)
Summary
State e2 nucleolar 60s ribosomal biogenesis intermediate - l1 stalk local model
Reference
Cruz VE, Sekulski K, Peddada N, Sailer C, Balasubramanian S, Weirich CS, Stengel F, Erzberger JP (2022): "Sequence-specific remodeling of a topologically complex RNP substrate by Spb4." Nat.Struct.Mol.Biol., 29, 1228-1238. doi: 10.1038/s41594-022-00874-9.
Abstract
DEAD-box ATPases are ubiquitous enzymes essential in all aspects of RNA biology. However, the limited in vitro catalytic activities described for these enzymes are at odds with their complex cellular roles, most notably in driving large-scale RNA remodeling steps during the assembly of ribonucleoproteins (RNPs). We describe cryo-EM structures of 60S ribosomal biogenesis intermediates that reveal how context-specific RNA unwinding by the DEAD-box ATPase Spb4 results in extensive, sequence-specific remodeling of rRNA secondary structure. Multiple cis and trans interactions stabilize Spb4 in a post-catalytic, high-energy intermediate that drives the organization of the three-way junction at the base of rRNA domain IV. This mechanism explains how limited strand separation by DEAD-box ATPases is leveraged to provide non-equilibrium directionality and ensure efficient and accurate RNP assembly.

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