5jcs
CRYO-EM STRUCTURE OF THE RIX1-REA1 PRE-60S PARTICLECRYO-EM STRUCTURE OF THE RIX1-REA1 PRE-60S PARTICLE
Structural highlights
FunctionPublication Abstract from PubMedRibosome synthesis is catalyzed by approximately 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 approximately 180 degrees 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. Architecture of the Rix1-Rea1 checkpoint machinery during pre-60S-ribosome remodeling.,Barrio-Garcia C, Thoms M, Flemming D, Kater L, Berninghausen O, Bassler J, Beckmann R, Hurt E Nat Struct Mol Biol. 2016 Jan;23(1):37-44. doi: 10.1038/nsmb.3132. Epub 2015 Nov , 30. PMID:26619264[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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