@article{,
title = {The nucle(ol)ar Tif6p and Efl1p are required for a late cytoplasmic step of ribosome synthesis},
author = {B Senger and D L Lafontaine and J S Graindorge and O Gadal and A Camasses and A Sanni and J M Garnier and M Breitenbach and E Hurt and F Fasiolo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11779510},
isbn = {11779510},
year = {2001},
date = {2001-01-01},
journal = {Mol Cell},
volume = {8},
number = {6},
pages = {1363-1373},
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.},
note = {1097-2765
Journal Article},
keywords = {Biological Transport Cell Division Cell Nucleolus/*metabolism Cell Nucleus/*metabolism Conserved Sequence Cytoplasm/enzymology/*metabolism Enzyme Activation GTP Phosphohydrolases/chemistry/genetics/*metabolism Gene Deletion Genes, Fungal/chemistry/genetics/metabolism RNA, Non-U.S. Gov't, Post-Transcriptional RNA, Reporter/genetics Molecular Weight Phenotype Protein Subunits RNA Precursors/chemistry/genetics/metabolism *RNA Processing, Ribosomal/chemistry/genetics/metabolism Ribosomes/chemistry/*metabolism Saccharomyces cerevisiae/cytology/genetics/growth & development/*metabolism Saccharomyces cerevisiae Proteins/chemistry/genetics/metabolism Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
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.