Nucleotide sequence analysis and immunoprecipitation revealed that the nucleolar Th RNP is identical to the RNA component of RNase MRP and structurally related to RNase P.
The study identifies that the nucleolar Th RNP is identical to the RNA processing enzyme RNase MRP and shares a common autoantigenic polypeptide with RNase P.
Sera from patients with autoimmune diseases often contain antibodies that bind ribonucleoproteins (RNPs). Sera from 30 such patients were found to immunoprecipitate ribonuclease P (RNase P), an RNP enzyme required to process the 5' termini of transfer RNA transcripts in nuclei and mitochondria of eukaryotic cells. All 30 sera also immunoprecipitated the nucleolar Th RNP, indicating that the two RNPs are structurally related. Nucleotide sequence analysis of the Th RNP revealed it was identical to the RNA component of the mitochondrial RNA processing enzyme known as RNase MRP. Antibodies that immunoprecipitated the Th RNP selectively depleted murine and human cell extracts of RNase MRP activity, indicating that the Th and RNase MRP RNPs are identical. Since RNase P and RNase MRP are not associated with each other during biochemical purification, we suggest that these two RNA processing enzymes share a common autoantigenic polypeptide.
Gold et al. (Fri,) conducted a other in Autoimmune diseases (n=30). Immunoprecipitation and nucleotide sequence analysis was evaluated on Identity and structural relationship of RNase P, Th RNP, and RNase MRP. Nucleotide sequence analysis and immunoprecipitation revealed that the nucleolar Th RNP is identical to the RNA component of RNase MRP and structurally related to RNase P.