Abstract:
: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.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
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 Hdoi
10.1128/MCB.00668-07subject
Has Abstractpub_date
2007-10-01 00:00:00pages
6581-92issue
19eissn
0270-7306issn
1098-5549pii
MCB.00668-07journal_volume
27pub_type
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