Details

Autor(en) / Beteiligte

• Dang, Y L
• Martin, N C

Titel

Yeast mitochondrial RNase P: sequence of the RPM2 gene and demonstration that its product is a protein subunit of the enzyme

Ist Teil von

• The Journal of biological chemistry, 1993-09, Vol.268 (26), p.19791-19796

Ort / Verlag

Bethesda, MD: American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1993

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• We report here the sequence of the RPM2 gene which codes for the 105-kDa protein previously purified from the mitochondria of Saccharomyces cerevisiae and shown by genetic techniques to be required for mitochondrial RNase P activity. The sequence predicts a primary translation product of 1202 residues with a molecular mass of 139 kDa and no obvious sequence similarity to any known protein in the data bases. There are 122 amino-terminal amino acids predicted by the gene that are not found in the purified protein, some of which may play a role in mitochondrial targeting of the protein. Antibodies raised against a trpE- 105-kDa fusion protein recognize a 105-kDa protein in wild-type cells but not in cells carrying a disruption of the RMP2 gene. Immune, but not preimmune serum, immunoprecipitates the RNase P RNA and the mitochondrial RNase P activity. Thus, the 105-kDa protein forms a complex with RNase P RNA and is required for RNase P activity as predicted for a bona fide subunit of the enzyme.