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Nucleic Acids Research, 2000, Vol. 28, No. 8 1684-1691
© 2000 Oxford University Press

Degradation of ribosomal RNA precursors by the exosome

Christine Allmang, Philip Mitchell, Elisabeth Petfalski and David Tollervey*

Institute of Cell and Molecular Biology, Swann Building, King’s Buildings, The University of Edinburgh, Mayfield Road, Edinburgh EH9 3JR, UK

The yeast exosome is a complex of 3'->5' exonucleases involved in RNA processing and degradation. All 11 known components of the exosome are required during 3' end processing of the 5.8S rRNA. Here we report that depletion of each of the individual components inhibits the early pre-rRNA cleavages at sites A0, A1, A2 and A3, reducing the levels of the 32S, 20S, 27SA2 and 27SA3 pre-rRNAs. The levels of the 27SB pre-rRNAs were also reduced. Consequently, both the 18S and 25S rRNAs were depleted. Since none of these processing steps involves 3'->5' exonuclease activities, the requirement for the exosome is probably indirect. Correct assembly of trans-acting factors with the pre-ribosomes may be monitored by a quality control system that inhibits pre-rRNA processing. The exosome itself degrades aberrant pre-rRNAs that arise from such inhibition. Exosome mutants stabilize truncated versions of the 23S, 21S and A2-C2 RNAs, none of which are observed in wild-type cells. The putative helicase Dob1p, which functions as a cofactor for the exosome in pre-rRNA processing, also functions in these pre-rRNA degradation activities.

* To whom correspondence should be addressed. Tel: +44 131 650 7092; Fax: +44 131 650 7040; Email: d.tollervey@ed.ac.uk The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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