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Vol. 12, Issue 11, 3680-3689, November 2001
Department of Biochemistry, University of Nijmegen, NL-6500 HB
Nijmegen, The Netherlands
The RNase MRP and RNase P ribonucleoprotein particles both function
as endoribonucleases, have a similar RNA component, and share several
protein subunits. RNase MRP has been implicated in pre-rRNA processing
and mitochondrial DNA replication, whereas RNase P functions in
pre-tRNA processing. Both RNase MRP and RNase P accumulate in the
nucleolus of eukaryotic cells. In this report we show that for three
protein subunits of the RNase MRP complex (hPop1, hPop4, and Rpp38)
basic domains are responsible for their nucleolar accumulation and that
they are able to accumulate in the nucleolus independently of their
association with the RNase MRP and RNase P complexes. We also show that
certain mutants of hPop4 accumulate in the Cajal bodies, suggesting
that hPop4 traverses through these bodies to the nucleolus.
Furthermore, we characterized a deletion mutant of Rpp38 that
preferentially associates with the RNase MRP complex, giving a first
clue about the difference in protein composition of the human RNase MRP
and RNase P complexes. On the basis of all available data on nucleolar
localization sequences, we hypothesize that nucleolar accumulation of
proteins containing basic domains proceeds by diffusion and retention
rather than by an active transport process. The existence of nucleolar
localization sequences is discussed.
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