Human mitochondrial RNase P does not distinguish itself from other RNase P enzymes by
most of its basic properties. 5′ phosphates on tRNA products, strict dependence on a …

A ribonuclease P-like activity was partially purified from HeLa cell mitochondria by DEAE-
cellulose and octyl-Sepharose chromatography. RNase P-like activity can be quantitatively …

Summary tRNAs are synthesized as immature precursors, and on their way to functional
maturity, extra nucleotides at their 5′ ends are removed by an endonuclease called RNase …

Mitochondrial tRNAs are generally synthesized as part of polycistronic transcripts. Release
of tRNAs from these precursors is thus not only required to produce functional adaptors for …

We have previously described a mitochondrial activity that removes 5′ leaders from yeast
mitochondrial precursor tRNAs and suggested that it is a mitochondrial RNase P. Here we …

The mitochondrion-associated RNase P activity (mtRNase P) was extensively purified from
HeLa cells and shown to reside in particles with a sedimentation constant (∼ 17S) very …

We previously demonstrated that mammalian cells contain at least two distinct RNase P
activities, one nuclear and one mitochondrial (5, 7). These enzymes were shown to have …

In bacteria, archaea, and the eukaryote nucleus, the endonuclease ribonuclease P (RNase
P) is composed of a catalytic RNA that is assisted by protein subunits. Holzmann et al.(2008) …

Transfer RNAs (tRNAs) reach their mature functional form through several steps of
processing and modification. Some nucleotide modifications affect the proper folding of …

RNase P from the mitochondria of Saccharomyces cerevisiae was purified to near
homogeneity> 1800-fold with a yield of 1.6% from mitochondrial extracts. The most …