Abstract:
:Analyses of isolated pre-ribosomes yielded biochemical "snapshots" of the dynamic, nascent 60S and 40S subunits during their path from the nucleolus to the cytoplasm. Here, we present the structure of a pre-60S ribosomal intermediate located in the nucleoplasm. A huge dynein-related AAA-type ATPase (Rea1) and the Rix1 complex (Rix1-Ipi1-Ipi3) are components of an extended (approximately 45 nm long) pre-60S particle. Antibody crosslinking in combination with electron microscopy revealed that the Rea1 localizes to the "tail" region and ribosomal proteins to the "head" region of the elongated "tadpole-like" structure. Furthermore, in vitro treatment with ATP induces dissociation of Rea1 from the pre-60S subunits. Rea1 and the Rix1 complex could mediate ATP-dependent remodeling of 60S subunits and subsequent export from the nucleoplasm to the cytoplasm.
journal_name
Mol Celljournal_title
Molecular cellauthors
Nissan TA,Galani K,Maco B,Tollervey D,Aebi U,Hurt Edoi
10.1016/j.molcel.2004.06.033subject
Has Abstractpub_date
2004-07-23 00:00:00pages
295-301issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(04)00376-4journal_volume
15pub_type
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