Co-purification of a small RNA species with multicatalytic proteinase (proteasome) from rat liver

Previous studies have come to different conclusions about the presence of RNA in particles known variously as prosomes, proteasomes or multicatalytic proteinase (MCP). To determine the reason for this, MCP was isolated from rat liver by 4 different purification protocols. One major band of RNA, abou...

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Bibliographic Details
Published in:FEBS letters 1991-02, Vol.279 (2), p.351-355
Main Authors: Skilton, Helen E., Eperon, Ian C., Rivett, A.Jennifer
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cysteine Endopeptidases - chemistry
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Liver - enzymology
Molecular Weight
Multicatalytic proteinase
Multienzyme Complexes - chemistry
Proteasome
Proteasome Endopeptidase Complex
Rats
Ribonucleoproteins - chemistry
RNA
RNA - analysis
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Summary:Previous studies have come to different conclusions about the presence of RNA in particles known variously as prosomes, proteasomes or multicatalytic proteinase (MCP). To determine the reason for this, MCP was isolated from rat liver by 4 different purification protocols. One major band of RNA, about 80 nucleotides in length, co-purified in all preparations. The amount of RNA detected was less than one molecule per MCP particle suggesting that there may be more than one population of MCP in rat liver cells.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(91)80185-6