A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunits |
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Authors: | Nissan Tracy A Galani Kyriaki Maco Bohumil Tollervey David Aebi Ueli Hurt Ed |
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Affiliation: | Biochemie-Zentrum der Universit?t Heidelberg, Im Neuenheimer Feld 328, 69120, Germany. |
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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. |
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