Abstract
The present work demonstrates the ability of 20S proteasome-containing, tightly bound to chromatin RNP-particles (alpha-RNP) to endonucleolyse specific messenger RNAs (in particular, human mRNA for p53 gene and mRNA for luciferase from Renilla sp.). The dependence of individual mRNA endonucleolysis by alpha-RNP particles on both the substrate and enzyme was found.
MeSH terms
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Chromatin / metabolism
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Cysteine Endopeptidases / analysis
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Cysteine Endopeptidases / metabolism*
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Endoribonucleases / metabolism*
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Genes, p53
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Humans
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K562 Cells / enzymology*
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Luciferases / genetics
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Multienzyme Complexes / analysis
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Multienzyme Complexes / metabolism*
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Proteasome Endopeptidase Complex
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RNA, Messenger / metabolism
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Ribonucleoproteins, Small Cytoplasmic / chemistry
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Ribonucleoproteins, Small Cytoplasmic / metabolism*
Substances
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Chromatin
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Multienzyme Complexes
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RNA, Messenger
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Ribonucleoproteins, Small Cytoplasmic
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Luciferases
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Endoribonucleases
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex