A Pre-Ribosome with a Tadpole-like Structure Functions in ATP-Dependent Maturation of 60S Subunits
Copyright policy )A Pre-Ribosome with a Tadpole-like Structure Functions in ATP-Dependent Maturation of 60S Subunits
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.
- Wellcome Centre for Cell Biology United Kingdom
- University of Edinburgh United Kingdom
- University of Basel Switzerland
- Heidelberg University Germany
Cytoplasm, Saccharomyces cerevisiae Proteins, Biological Transport, Active, Cell Biology, Saccharomyces cerevisiae, Microscopy, Electron, Adenosine Triphosphate, Cross-Linking Reagents, RNA, Ribosomal, Immunoglobulin G, RNA Precursors, Molecular Biology, Ribosomes, Cell Nucleolus
Cytoplasm, Saccharomyces cerevisiae Proteins, Biological Transport, Active, Cell Biology, Saccharomyces cerevisiae, Microscopy, Electron, Adenosine Triphosphate, Cross-Linking Reagents, RNA, Ribosomal, Immunoglobulin G, RNA Precursors, Molecular Biology, Ribosomes, Cell Nucleolus
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