A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunits.

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 Cell

journal_title

Molecular cell

authors

Nissan TA,Galani K,Maco B,Tollervey D,Aebi U,Hurt E

doi

10.1016/j.molcel.2004.06.033

subject

Has Abstract

pub_date

2004-07-23 00:00:00

pages

295-301

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(04)00376-4

journal_volume

15

pub_type

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