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Cytoplasmic recycling of 60S preribosomal factors depends on the AAA protein Drg1.

Allelic forms of DRG1/AFG2 confer resistance to the drug diazaborine, an inhibitor of ribosome biogenesis in Saccharomyces cerevisiae. Our results show that the AAA-ATPase Drg1 is essential for 60S maturation and associates with 60S precursor particles in the cytoplasm. Functional inactivation of Drg1 leads to an increased cytoplasmic localization of shuttling pre-60S maturation factors like Rlp24, Arx1, and Tif6. Surprisingly, Nog1, a nuclear pre-60S factor, was also relocalized to the cytoplasm under these conditions, suggesting that it is a previously unsuspected shuttling preribosomal factor that is exported with the precursor particles and very rapidly reimported. Proteins that became cytoplasmic under drg1 mutant conditions were blocked on pre-60S particles at a step that precedes the association of Rei1, a later-acting preribosomal factor. A similar cytoplasmic accumulation of Nog1 and Rlp24 in pre-60S-bound form could be seen after overexpression of a dominant-negative Drg1 variant mutated in the D2 ATPase domain. We conclude that the ATPase activity of Drg1 is required for the release of shuttling proteins from the pre-60S particles shortly after their nuclear export. This early cytoplasmic release reaction defines a novel step in eukaryotic ribosome maturation.

Pubmed ID: 17646390


  • Pertschy B
  • Saveanu C
  • Zisser G
  • Lebreton A
  • Tengg M
  • Jacquier A
  • Liebminger E
  • Nobis B
  • Kappel L
  • van der Klei I
  • Högenauer G
  • Fromont-Racine M
  • Bergler H


Molecular and cellular biology

Publication Data

October 17, 2007

Associated Grants


Mesh Terms

  • Adenosine Triphosphatases
  • Biological Transport
  • Carrier Proteins
  • Cytoplasm
  • GTP-Binding Proteins
  • Intermediate Filament Proteins
  • Nuclear Proteins
  • Peptide Initiation Factors
  • Phosphoproteins
  • Protein Precursors
  • Recombinant Fusion Proteins
  • Ribosomal Proteins
  • Ribosome Subunits, Large, Eukaryotic
  • Ribosomes
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins