5JCS

CRYO-EM STRUCTURE OF THE RIX1-REA1 PRE-60S PARTICLE

This is a non-PDB format compatible entry.

Replaces:  5FL8

Summary for 5JCS

• Entry DOI: 10.2210/pdb5jcs/pdb
• EMDB information: 3199
• Descriptor: 60S ribosomal protein L2-A, 60S ribosomal protein L34-A, 60S ribosomal protein L7-A, ... (48 entities in total)
• Functional Keywords: pre-60s ribosome rix1 rea1, ribosome
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 48
• Total formula weight: 2814398.17

Authors

Barrio-Garcia, C.,Thoms, M.,Flemming, D.,Kater, L.,Berninghausen, O.,Bassler, J.,Beckmann, R.,Hurt, E. (deposition date: 2016-04-15, release date: 2016-11-16, Last modification date: 2024-07-10)

Primary citation

Barrio-Garcia, C.,Thoms, M.,Flemming, D.,Kater, L.,Berninghausen, O.,Bassler, J.,Beckmann, R.,Hurt, E.
Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome remodeling
Nat.Struct.Mol.Biol., 23:37-44, 2016

PubMed 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.

PubMed: 26619264
DOI: 10.1038/nsmb.3132

Experimental method

ELECTRON MICROSCOPY (9.5 Å)