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Vol. 95, Issue 12, 6716-6721, June 9, 1998

Biochemistry
 Rpp2, an essential protein subunit of nuclear RNase P, is required for processing of precursor tRNAs and 35S precursor rRNA in Saccharomyces cerevisiae

Viktor Stolc*, Alexander Katzdagger , and Sidney Altmandagger ,Dagger

dagger  Department of Biology, Yale University, New Haven, CT 06520; and * Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510

Contributed by Sidney Altman, March 31, 1998

RPP2, an essential gene that encodes a 15.8-kDa protein subunit of nuclear RNase P, has been identified in the genome of Saccharomyces cerevisiae. Rpp2 was detected by sequence similarity with a human protein, Rpp20, which copurifies with human RNase P. Epitope-tagged Rpp2 can be found in association with both RNase P and RNase mitochondrial RNA processing in immunoprecipitates from crude extracts of cells. Depletion of Rpp2 protein in vivo causes accumulation of precursor tRNAs with unprocessed introns and 5' and 3' termini, and leads to defects in the processing of the 35S precursor rRNA. Rpp2-depleted cells are defective in processing of the 5.8S rRNA. Rpp2 immunoprecipitates cleave both yeast precursor tRNAs and precursor rRNAs accurately at the expected sites and contain the Rpp1 protein orthologue of the human scleroderma autoimmune antigen, Rpp30. These results demonstrate that Rpp2 is a protein subunit of nuclear RNase P that is functionally conserved in eukaryotes from yeast to humans.

Dagger    To whom reprint requests should be addressed. e-mail: sidney.altman{at}qm.yale.edu.

Copyright © 1998 by The National Academy of Sciences  0027-8424/98/956716-6$2.00/0
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