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A Functional Dominant Mutation in Schizosaccharomyces Pombe RNase MRP RNA Affects Nuclear RNA Processing and Requires the Mitochondrial-associated Nuclear Mutation Ptp1-1 for Viability

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Journal EMBO J
Date 1996 Sep 2
PMID 8887563
Citations 9
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Abstract

The essential gene for RNase MRP RNA, mrp1, was identified previously in Schizosaccharomyces pombe by homology to mammalian RNase MRP RNAs. Here we describe distinct site-specific mutations in RNase MRP RNA that support a conserved role for this ribonucleoprotein in nucleolar 5.8S rRNA processing. One characterized mutation, mrp1-ND90, displays dominance and results in accumulation of unspliced precursor RNAs of dimeric tRNA(Ser)-tRNA(Met)i, suggesting a novel nuclear role for RNase MRP in tRNA processing. Cells carrying the mrp1-ND90 mutation, in the absence of a wild-type copy of mrp1, additionally require the mitochondrially associated nuclear mutation ptp1-1 for viability. Analysis of this mrp1 mutation reinforces previous biochemical evidence suggesting a role for RNase MRP in mitochondrial DNA replication. Several mutations in mrp1 result in unusual cellular morphology, including alterated nuclear organization, and are consistent with a broader nuclear role for RNase MRP in regulating a nuclear signal for septation; these results are a further indication of the multifunctional nature of this ribonucleoprotein.

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References
1.
Rubin G . Three forms of the 5.8-S ribosomal RNA species in Saccharomyces cerevisiae. Eur J Biochem. 1974; 41(1):197-202. DOI: 10.1111/j.1432-1033.1974.tb03260.x. View

2.
Morrissey J, Tollervey D . Birth of the snoRNPs: the evolution of RNase MRP and the eukaryotic pre-rRNA-processing system. Trends Biochem Sci. 1995; 20(2):78-82. DOI: 10.1016/s0968-0004(00)88962-8. View

3.
Bothwell A, Garber R, Altman S . Nucleotide sequence and in vitro processing of a precursor molecule to Escherichia coli 4.5 S RNA. J Biol Chem. 1976; 251(23):7709-16. View

4.
Mao J, Appel B, Schaack J, Sharp S, Yamada H, Soll D . The 5S RNA genes of Schizosaccharomyces pombe. Nucleic Acids Res. 1982; 10(2):487-500. PMC: 326152. DOI: 10.1093/nar/10.2.487. View

5.
Hashimoto C, Steitz J . Sequential association of nucleolar 7-2 RNA with two different autoantigens. J Biol Chem. 1983; 258(3):1379-82. View