期刊
MOLECULAR CELL
卷 38, 期 5, 页码 712-721出版社
CELL PRESS
DOI: 10.1016/j.molcel.2010.05.024
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资金
- Deutsche Forschungsgemeinschaft [Hu363/9-2]
- Fonds der Chemischen Industrie
- Austrian Science Fund (FWF) [T404-B12]
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, Ytml, via a related motif. In vivo Rea1 contacts Ytml before it contacts Rsa4, and its interaction with Ytml 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.
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