Drosophila small cytoplasmic 19S ribonucleoprotein is homologous to the rat multicatalytic proteinase.
All eukaryotic cells so far analysed contain 19S particles which share a cylinder-like shape and are composed of a set of proteins of relative molecular mass ranging typically from 19,000 to 36,000 (refs 1-10). Proposed functions have included synthetase activity, transfer RNA processing or messenger RNA repression, but their biological importance remains obscure. A multicatalytic proteinase (MCP) of similar size and shape has been isolated from mammalian tissues. The apparent similarities of these high molecular weight complexes suggest a biochemical and functional homology between the small cytoplasmic 19S particle from Drosophila melanogaster (19S-scRNP) (ref. 7) and rat MCP (ref. 14). By means of electron microscopy, immunological techniques, RNA identification and proteinase activity assays, we were able to show that the two structurally similar complexes are immunologically related ribonucleoproteins (RNPs) with similar proteolytic activity.
D000818:Animals; D003546:Cysteine Endopeptidases / Q000235:genetics*; D003593:Cytoplasm / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000235:genetics*; D046988:Proteasome Endopeptidase Complex; D051381:Rats / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000235:genetics* / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid
D009097:Multienzyme Complexes; D012261:Ribonucleoproteins; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex