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Originally published as MBC in Press, 10.1091/mbc.E07-10-1015 on January 30, 2008

Vol. 19, Issue 4, 1499-1508, April 2008

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Inactivation of Cleavage Factor I Components Rna14p and Rna15p Induces Sequestration of Small Nucleolar Ribonucleoproteins at Discrete Sites in the Nucleus

Tiago Carneiro*,{dagger}, Célia Carvalho*, José Braga*, José Rino*, Laura Milligan{ddagger}, David Tollervey{ddagger}, and Maria Carmo-Fonseca*

*Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa, 1649-028 Lisboa, Portugal; and {ddagger}Wellcome Trust Centre for Cell Biology, University of Edinburgh, EH9 3JR, United Kingdom

Submitted October 9, 2007; Revised January 7, 2008; Accepted January 18, 2008
Monitoring Editor: A. Gregory Matera

Small nucleolar RNAs (snoRNAs) associate with specific proteins forming small nucleolar ribonucleoprotein (snoRNP) particles, which are essential for ribosome biogenesis. The snoRNAs are transcribed, processed, and assembled in snoRNPs in the nucleoplasm. Mature particles are then transported to the nucleolus. In yeast, 3'-end maturation of snoRNAs involves the activity of Rnt1p endonuclease and cleavage factor IA (CFIA). We report that after inhibition of CFIA components Rna14p and Rna15p, the snoRNP proteins Nop1p, Nop58p, and Gar1p delocalize from the nucleolus and accumulate in discrete nucleoplasmic foci. The U14 snoRNA, but not U3 snoRNA, similarly redistributes from the nucleolus to the nucleoplasmic foci. Simultaneous depletion of either Rna14p or Rna15p and the nuclear exosome component Rrp6p induces accumulation of poly(A)+ RNA at the snoRNP-containing foci. We propose that the foci detected after CFIA inactivation correspond to quality control centers in the nucleoplasm.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/10.1091/mbc.E07-10-1015) on January 30, 2008.

{dagger} Present address: Instituto Gulbenkian de Ciência, Oeiras, Portugal.

Address correspondence to: Maria Carmo-Fonseca (carmo.fonseca{at}fm.ul.pt).






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