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 fac...
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| Hauptverfasser: | , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2010 June 11
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| In: |
Molecular cell
Year: 2010, Jahrgang: 38, Heft: 5, Pages: 712-721 |
| ISSN: | 1097-4164 |
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| Verfasserangaben: | Jochen Bassler, Martina Kallas, Brigitte Pertschy, Cornelia Ulbrich, Matthias Thoms, and Ed Hurt |
| Zusammenfassung: | 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. |
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| Beschreibung: | Gesehen am 07.12.2022 |
| Beschreibung: | Online Resource |
| ISSN: | 1097-4164 |