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Published online June 16, 2008
doi:10.1083/jcb.200801181
The Journal of Cell Biology, Vol. 181, No. 6, 935-944
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Kressler et al.
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Article

 The AAA ATPase Rix7 powers progression of ribosome biogenesis by stripping Nsa1 from pre-60S particles

Dieter Kressler, Daniela Roser, Brigitte Pertschy, and Ed Hurt

Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany

Correspondence to E. Hurt: ed.hurt{at}bzh.uni-heidelberg.de

Ribosome biogenesis takes place successively in the nucleolar, nucleoplasmic, and cytoplasmic compartments. Numerous nonribosomal factors transiently associate with the nascent ribosomes, but the mechanisms driving ribosome formation are mostly unknown. Here, we show that an energy-consuming enzyme, the AAA-type (ATPases associated with various cellular activities) ATPase Rix7, restructures a novel pre-60S particle at the transition from the nucleolus to nucleoplasm. Rix7 interacts genetically with Nsa1 and is targeted to the Nsa1-defined preribosomal particle. In vivo, Nsa1 cannot dissociate from pre-60S particles in rix7 mutants, causing nucleolar Nsa1 to escape to the cytoplasm, where it remains associated with aberrant 60S subunits. Altogether, our data suggest that Rix7 is required for the release of Nsa1 from a discrete preribosomal particle, thereby triggering the progression of 60S ribosome biogenesis.

Abbreviations used in this paper: AAA, ATPases associated with various cellular activities; pre-rRNA, precursor rRNA; rRNA, ribosomal RNA; SDC, synthetic dextrose complete; sl, synthetic lethal; TAP, tandem affinity purification; ts, temperature sensitive.


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