Senger B, Lafontaine D L, Graindorge J S, Gadal O, Camasses A, Sanni A, Garnier J M, Breitenbach M, Hurt E, Fasiolo F
UPR no 9002 du CNRS, Institut de Biologie Moleculaire et Cellulaire du CNRS, 15 Rue Rene Descartes, 67084 Strasbourg Cedex, France.
Mol Cell. 2001 Dec;8(6):1363-73. doi: 10.1016/s1097-2765(01)00403-8.
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.
与核糖体转位酶EF-G/EF-2同源的细胞质GTP酶延伸因子样1（Efl1p）的缺失会导致核仁前体rRNA加工和60S前体亚基输出缺陷。Efl1p与Tif6p发生遗传相互作用，Tif6p是一种与60S前体亚基稳定相关的核仁蛋白，其合成和核输出都需要它。在没有Efl1p的情况下，50%的Tif6p会重新定位于细胞质。在体外，Efl1p的GTP酶活性受到60S的刺激，并且Efl1p促进Tif6p-60S复合物的解离。我们提出，Tif6p在核仁中与60S前体亚基结合，并将它们护送至细胞质，在那里Efl1p的GTP酶活性触发后期结构重排，这有助于Tif6p的释放及其向核仁的循环利用。
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