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PMID: 3537697 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

RNase P activity in the mitochondria of Saccharomyces cerevisiae depends on both mitochondrion and nucleus-encoded components.

Molecular and cellular biology ·Vol. 6 ·No. 4 ·1986-04-00 ·Pages 1058-64

Hollingsworth MJ, Martin NC

Abstract

A requisite step in the biosynthesis of tRNA is the removal of 5' leader sequences from tRNA precursors. We have detected an RNase P activity in yeast mitochondrial extracts that can carry out this reaction on a homologous precursor tRNA. This mitochondrial RNase P was sensitive to both micrococcal nuclease and protease, demonstrating that it requires both a nucleic acid and protein for activity. The presence of RNase P activity in vitro directly correlated with the presence of a locus on yeast mitochondrial DNA previously shown by genetic and biochemical studies to be required for tRNA maturation. The product of the locus, the 9S RNA, and this newly described mitochondrial RNase P activity cofractionated, providing further evidence that the 9S RNA is the RNA component of yeast mitochondrial RNase P.

MeSH Terms
Cell Nucleus/metabolism Endoribonucleases/isolation & purification,metabolism Micrococcal Nuclease/metabolism Mitochondria/enzymology Nucleic Acid Hybridization RNA, Transfer/genetics Ribonuclease P Saccharomyces cerevisiae/enzymology
Chemicals
RNA, Transfer Endoribonucleases Ribonuclease P Micrococcal Nuclease
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Hollingsworth M J
Martin N C
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.6.4.1058-1064.1986
Published
1986-04-00
Pages
1058-64
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC367615
Subset
IM
External Links
PubMed source DOI: 10.1128/mcb.6.4.1058-1064.1986 PMC Full Text View journal details
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