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Science 22 September 1989:
Vol. 245. no. 4924, pp. 1377 - 1380
DOI: 10.1126/science.2476849
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Articles

Science, Vol 245, Issue 4924, 1377-1380
Copyright © 1989 by American Association for the Advancement of Science

articles

The RNA processing enzyme RNase MRP is identical to the Th RNP and related to RNase P

HA Gold, JN Topper, DA Clayton, and J Craft

Department of Medicine, Yale University School of Medicine, New Haven, CT 06511.

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.


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