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. 2001 Dec;8(6):1363-73.
doi: 10.1016/s1097-2765(01)00403-8.

The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis

B Senger  1 , D L Lafontaine, J S Graindorge, O Gadal, A Camasses, A Sanni, J M Garnier, M Breitenbach, E Hurt, F Fasiolo
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Free article

The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis

B Senger et al. Mol Cell. 2001 Dec.
Free article

Abstract

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.

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