Publication Date:
1984-12-14
Description:
A cytoplasmic RNA moiety is necessary for posttranslational uptake of nuclear-encoded mammalian proteins destined for the mitochondrial matrix. Post-translational addition of ribonuclease to a reticulocyte lysate-programmed cell-free translation mixture inhibited subsequent import of six different mitochondrial matrix enzyme precursors into rat liver mitochondria. The required RNA is highly protected, as indicated by the high concentrations of ribonuclease necessary to produce this inhibition. The dependence of the inhibitory effect on temperature, duration of exposure to ribonuclease, and availability of divalent cations is characteristic of the nuclease susceptibility of ribonucleoproteins. The ribonuclease-sensitive component was found in a 400-kilodalton fraction which contains the mitochondrial protein precursors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Firgaira, F A -- Hendrick, J P -- Kalousek, F -- Kraus, J P -- Rosenberg, L E -- AM 09527/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Dec 14;226(4680):1319-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6209799" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Cell-Free System
;
Cytoplasm/metabolism
;
Mitochondria, Liver/*metabolism
;
Ornithine Carbamoyltransferase/metabolism
;
Protein Precursors/*metabolism
;
*Protein Processing, Post-Translational
;
RNA/*metabolism
;
Rats
;
Ribonucleases/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
