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Nucleic Acids Research, Vol 24, Issue 16 3158-3166, Copyright © 1996 by Oxford University Press
JR Chamberlain, , DW Kindelberger and DR Engelke
RNase P is a ribonucleoprotein endoribonuclease responsible for the 5'
maturation of precursor tRNAs in all organisms. While analyzing mutations
in conserved positions of the yeast nuclear RNase P RNA subunit,
significant accumulation of an aberrant RNA of approximately 193
nucleotides was observed. This abundant RNA was identified as a 3'extended
form of the 5.8S rRNA. This strain also displays a slightly elevated level
of other rRNA processing intermediates with 5-ends at processing site A2 in
the internal transcribed spacer 1 (ITS1) region of the rRNA primary
transcript. To test whether pre-rRNA in the region of ITS1/5.8S/ITS2 is a
substrate for RNase P in vitro, nuclear RNase P was partially purified to
remove contaminating nucleases. Cleavage assays were performed using an
rRNA substrate transcribed in vitro which includes the 5.8S region and its
surrounding processing sites in ITS1 and ITS2. Discrete cleavages of this
rRNA substrate were coincident with the peak fractions of nuclear RNase P,
but not with fractions corresponding to mitochondrial RNase P or
ribonuclease MRP RNA. The cleavage activity is sensitive to treatment with
micrococcal nuclease, also consistent with an activity attributable to
RNase R The strong RNase P cleavage sites were mapped and their possible
relationships to steps in the rRNA processing pathway are considered. These
observations suggest an intimate relationship between the processes of tRNA
and rRNA maturation in the eukaryotic nucleus.
ARTICLES
An RNase P RNA subunit mutation affects ribosomal RNA processing
Program in Cellular and Molecular Biology, University of Michigan Medical School, Ann Arbor 48109-0606, USA.
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