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The RNA Component of Mitochondrial Ribonuclease P from Aspergillus Nidulans
Author(s) -
Lee Young Chul,
Lee Byeong Jae,
Kang Hyen Sam
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.00297.x
Subject(s) - rna , rnase p , rnase mrp , biology , rnase h , microbiology and biotechnology , ribonuclease iii , ribonuclease , gene , rna editing , rnase ph , primer extension , genetics , rna interference
Several RNA molecules that copurified with Aspergillus nidulans mitochondrial ribonuclease (RNase) P were identified [Lee, Y. C., Lee, B. J., Hwang, D. S. & Kang, H. S. (1996) Eur. J. Biochem. 235 , 289–296], and their partial sequences were determined. 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. The gene is extremely (A+T)‐rich and contains two regions of sequence similarity conserved among the known mitochondrial RNase P‐RNAs and the eubacterial RNase P‐RNAs. The determination of 5′ and 3′ termini by primer extension and sequencing indicated that the length of the RNA transcript is 232 nucleotides. Northern‐blot analysis revealed that its only subcellular location was the mitochondria. Two RNase P‐RNA fragments of 110 nucleotides and 80 nucleotides, each containing one of the two conserved regions, could be recovered from the nuclease‐treated enzyme without significant loss of activity. The sizes of these fragments appeared to be the minimum lengths required for the vitro activity of the enzyme.

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