Characterization of an Endoribonuclease in Rat-Liver Nucleoli
| Autor: | Wlodzimierz Szer, Amal Boctor, Albert Grossman |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Male
Poly U Nucleolus Endoribonuclease Biology Tritium medicine.disease_cause Coliphages Biochemistry Reovirus RNA Ribonucleases medicine Animals Chemical Precipitation Carbon Radioisotopes Escherichia coli chemistry.chemical_classification Deoxyribonucleases Hydrolysis RNA Ribosomal RNA Endonucleases Molecular biology Rats RNA Bacterial Enzyme Liver Solubility chemistry RNA Ribosomal Chromatography Gel RNA Viral Ultracentrifuge Ultracentrifugation Cell Nucleolus HeLa Cells |
| Zdroj: | European Journal of Biochemistry. 44:391-400 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1974.tb03496.x |
| Popis: | Synthetic RNAs, i.e. [3H]poly(U) and [14C]poly(A), and natural RNAs, i.e. 16-S and 23-S Escherichia coli ribosomal [14C]RNA and MS2 coliphage [3H]RNA, were incompletely hydrolyzed by a rat liver nucleolar enzyme as measured by solubilization of radioactivity following ethanol precipitation. Sucrose density gradient analysis of these RNA substrates following incubation with isolated rat liver nucleoli at 36 °C for 15 min demonstrated extensive shifts in their sedimentation coefficients. These data were taken as evidence that the nueleolar enzyme is an endoribonuclease. The enzyme has been solubilized and partially purified. The enzyme has no effect on intact double-stranded reovirus RNA. It cleaves 45-S HeLa precursor rRNA through a series of intermediate fragments of decreasing size to limit 4-S end products. Among other characteristics, this nucleolar endoribonuclease prefers single to multi-stranded RNA and is inhibited by DNAase. |
| Databáze: | OpenAIRE |
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