Summary information and primary citation
- PDB-id
-
5jcs;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ribosome
- Method
- cryo-EM (9.5 Å)
- Summary
- cryo-EM structure of the rix1-rea1 pre-60s
particle
- Reference
-
Barrio-Garcia C, Thoms M, Flemming D, Kater L,
Berninghausen O, Bassler J, Beckmann R, Hurt E (2016):
"Architecture
of the Rix1-Rea1 checkpoint machinery during
pre-60S-ribosome remodeling."
Nat.Struct.Mol.Biol., 23,
37-44. doi: 10.1038/nsmb.3132.
- Abstract
- Ribosome synthesis is catalyzed by ∼200 assembly
factors, which facilitate efficient production of mature
ribosomes. Here, we determined the cryo-EM structure of a
Saccharomyces cerevisiae nucleoplasmic pre-60S particle
containing the dynein-related 550-kDa Rea1 AAA(+) ATPase
and the Rix1 subcomplex. This particle differs from its
preceding state, the early Arx1 particle, by two massive
structural rearrangements: an ∼180° rotation of the 5S
ribonucleoprotein complex and the central protuberance (CP)
rRNA helices, and the removal of the 'foot' structure from
the 3' end of the 5.8S rRNA. Progression from the Arx1 to
the Rix1 particle was blocked by mutational perturbation of
the Rix1-Rea1 interaction but not by a dominant-lethal Rea1
AAA(+) ATPase-ring mutant. After remodeling, the Rix1
subcomplex and Rea1 become suitably positioned to sense
correct structural maturation of the CP, which allows
unidirectional progression toward mature ribosomes.