Disease relevance of RPM1

• We apply synchrotron-based small-angle X-ray scattering to investigate the relationship between compaction, metal binding, and structure formation of two RNAs at 37 degrees C: the 76 nucleotide yeast tRNA(Phe) and the 255 nucleotide catalytic domain of the Bacillus subtilis RNase P RNA [1].
• Differences in the interaction of Escherichia coli RNase P RNA with tRNAs containing a short or a long extra arm [2].

High impact information on RPM1

• Furthermore, strains with mutant RPM1 genes also accumulate precursor Rpm1r, suggesting that mutations in either gene can lead to similar biogenesis defects [3].
• A gene required for RNase P activity in Candida (Torulopsis) glabrata mitochondria codes for a 227-nucleotide RNA with homology to bacterial RNase P RNA [4].
• The gene is extremely AT rich and codes for AU-rich RNAs that display some sequence homology with the mitochondrial RNase P RNA from S. cerevisiae, including two regions of striking sequence homology between the mitochondrial RNAs and the bacterial RNase P RNAs [4].
• DNA sequence analysis of the mitochondrial DNA from the region coding for this RNA revealed a second conserved sequence block characteristic of RNase P RNA genes and the presence of a downstream tRNA(Pro) gene [5].
• In this study, a new promoter (SP) between the tRNA(fMet) and RNase P RNA genes has been identified which may participate in RNase P RNA gene expression [6].

Biological context of RPM1

• Despite a growing literature on the folding of RNA, our understanding of tertiary folding in large RNAs derives from studies on a small set of molecular examples, with primary focus on group I introns and RNase P RNA [7].
• Mg2+-dependent compaction and folding of yeast tRNAPhe and the catalytic domain of the B. subtilis RNase P RNA determined by small-angle X-ray scattering [1].
• Characterization of conserved sequence elements in eukaryotic RNase P RNA reveals roles in holoenzyme assembly and tRNA processing [8].
• An essential protein-binding domain of nuclear RNase P RNA [9].
• Selection of functional genes in vivo identified permissible variations, and viable clones that caused yeast to exhibit conditional growth phenotypes were tested for defects in RNase P RNA and tRNA biosynthesis [9].

Associations of RPM1 with chemical compounds

• The susceptibility of the isolates to fluconazole, ketoconazole and itraconazole, was measured by the agar diffusion method (E-test), using RPM1 1,640 medium with 2% glucose and phosphate buffer [10].
• 4-Thiouridine, a photoreactive analogue of uridine, was randomly incorporated into yeast tRNA(Phe) precursor molecules by transcription with T7 RNA polymerase and the resulting transcripts were converted into mature tRNA(Phe) by treatment with RNase P RNA [11].

Other interactions of RPM1

• Using an oligonucleotide probe, we cloned and mapped the gene encoding this putative RNA component of RNase P (RNase P-RNA), situated between URFA3 (unidentified reading frame A3) and cobA (apocytochrome b) genes in the mitochondrial genome of A. nidulans [12].

Analytical, diagnostic and therapeutic context of RPM1

• Sequence analysis of Saccharomyces exiguus mitochondrial DNA reveals an RNase P RNA gene flanked by two tRNA genes [13].
• A gel retardation assay allowed us to separate RNase P RNA pools into tRNA-binding and nonbinding fractions [14].

References