par Senger, B;Lafontaine, Denis 
;Graindorge, J S;Gadal, O;Camasses, A;Sanni, A;Garnier, Josette;Breitenbach, Michael;Hurt, Eduard C.;Fasiolo, F
Référence Molecular cell, 8, 6, page (1363-1373)
Publication Publié, 2001-12
;Graindorge, J S;Gadal, O;Camasses, A;Sanni, A;Garnier, Josette;Breitenbach, Michael;Hurt, Eduard C.;Fasiolo, FRéférence Molecular cell, 8, 6, page (1363-1373)
Publication Publié, 2001-12
Article révisé par les pairs
| Résumé : | Deletion of elongation factor-like 1 (Efl1p), a cytoplasmic GTPase homologous to the ribosomal translocases EF-G/EF-2, results in nucle(ol)ar pre-rRNA processing and pre-60S subunits export defects. Efl1p interacts genetically with Tif6p, a nucle(ol)ar protein stably associated with pre-60S subunits and required for their synthesis and nuclear exit. In the absence of Efl1p, 50% of Tif6p is relocated to the cytoplasm. In vitro, the GTPase activity of Efl1p is stimulated by 60S, and Efl1p promotes the dissociation of Tif6p-60S complexes. We propose that Tif6p binds to the pre-60S subunits in the nucle(ol)us and escorts them to the cytoplasm where the GTPase activity of Efl1p triggers a late structural rearrangement, which facilitates the release of Tif6p and its recycling to the nucle(ol)us. |
