The AAA-ATPase Rea1 drives removal of biogenesis factors during multiple stages of 60S ribosome assembly.
The AAA(+)-ATPase Rea1 removes the ribosome biogenesis factor Rsa4 from pre-60S ribosomal subunits in the nucleoplasm to drive nuclear export of the subunit. To do this, Rea1 utilizes a MIDAS domain to bind a conserved motif in Rsa4. Here, we show that the Rea1 MIDAS domain binds another pre-60S factor, ... Ytm1, via a related motif. In vivo Rea1 contacts Ytm1 before it contacts Rsa4, and its interaction with Ytm1 coincides with the exit of early pre-60S particles from the nucleolus to the nucleoplasm. In vitro, Rea1's ATPase activity triggers removal of the conserved nucleolar Ytm1-Erb1-Nop7 subcomplex from isolated early pre-60S particle. We suggest that the Rea1 AAA(+)-ATPase functions at successive maturation steps to remove ribosomal factors at critical transition points, first driving the exit of early pre-60S particles from the nucleolus and then driving late pre-60S particles from the nucleus.
Mesh Terms:
Adenosine Triphosphatases, Cell Nucleolus, Microtubule-Associated Proteins, Nuclear Proteins, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Ribosomal Proteins, Ribosome Subunits, Large, Eukaryotic, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques
Adenosine Triphosphatases, Cell Nucleolus, Microtubule-Associated Proteins, Nuclear Proteins, Protein Binding, Protein Structure, Tertiary, Recombinant Fusion Proteins, Ribosomal Proteins, Ribosome Subunits, Large, Eukaryotic, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Two-Hybrid System Techniques
Mol. Cell
Date: Jun. 11, 2010
PubMed ID: 20542003
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