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© The Rockefeller University Press, 0021-9525/2002/6/941 $5.00
The Journal of Cell Biology, Volume 157, Number 6, June 10, 2002 941-952

Rlp7p is associated with 60S preribosomes, restricted to the granular component of the nucleolus, and required for pre-rRNA processing

¹ BZH, Biochemie-Zentrum Heidelberg, D-69120 Heidelberg, Germany
² Wellcome Trust Centre for Cell Biology, University of Edinburgh, Swann Building, Edinburgh EH9 3JR, UK
³ Laboratoire de Biologie Moleculaire Eucaryote, F-32062 Toulouse, France

Address correspondence to Eduard Hurt, Biochemie-Zentrum Heidelberg (BZH), Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany. Tel.: 49-6221-54-4173. Fax: 49-6221-54-4369. E-mail: cg5{at}ix.urz.uni-heidelberg.de

Many analyses have examined subnucleolar structures in eukaryotic cells, but the relationship between morphological structures, pre-rRNA processing, and ribosomal particle assembly has remained unclear. Using a visual assay for export of the 60S ribosomal subunit, we isolated a ts-lethal mutation, rix9-1, which causes nucleolar accumulation of an Rpl25p-eGFP reporter construct. The mutation results in a single amino acid substitution (F₁₇₆S) in Rlp7p, an essential nucleolar protein related to ribosomal protein Rpl7p. The rix9-1 (rlp7-1) mutation blocks the late pre-RNA cleavage at site C₂ in ITS2, which separates the precursors to the 5.8S and 25S rRNAs. Consistent with this, synthesis of the mature 5.8S and 25S rRNAs was blocked in the rlp7-1 strain at nonpermissive temperature, whereas 18S rRNA synthesis continued. Moreover, pre-rRNA containing ITS2 accumulates in the nucleolus of rix9-1 cells as revealed by in situ hybridization. Finally, tagged Rlp7p was shown to associate with a pre-60S particle, and fluorescence microscopy and immuno-EM localized Rlp7p to a subregion of the nucleolus, which could be the granular component (GC). All together, these data suggest that pre-rRNA cleavage at site C₂ specifically requires Rlp7p and occurs within pre-60S particles located in the GC region of the nucleolus.

Key Words: rRNA processing; ribosome biogenesis; ribosome export; nucleolus; preribosome

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