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A pre-ribosome with a tadpole-like structure functions in ATP-dependent maturation of 60S subunits
Biochemie-Zentrum der Universität Heidelberg.
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2004 (English)In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 15, no 2, 295-301 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2004. Vol. 15, no 2, 295-301 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:umu:diva-46253DOI: 10.1016/j.molcel.2004.06.033PubMedID: 15260980OAI: oai:DiVA.org:umu-46253DiVA: diva2:437508
Available from: 2011-08-29 Created: 2011-08-29 Last updated: 2017-12-08Bibliographically approved

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