3′-immature tRNATrp is required for ribosome inactivation by gelonin,a plant RNA N-glycosidase
| Autor: | M. Denaro, Alessandra Pallanca, Paola Alvergna, Lucio Montanaro, Domenica Carnicelli, Maurizio Brigotti, Simonetta Sperti, R Lorenzetti |
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| Rok vydání: | 1995 |
| Předmět: |
Glycoside Hydrolases
RNase P Molecular Sequence Data Biochemistry Ribosome Animals Gelonin RNase H Molecular Biology Plant Proteins Protein Synthesis Inhibitors Binding Sites Base Sequence biology RNA RNA Probes Cell Biology Plants RNA Transfer Trp Molecular biology RNA editing Transfer RNA Ribosome Inactivating Proteins Type 1 biology.protein Cattle Electrophoresis Polyacrylamide Gel Ribosomes Sequence Alignment tRNA nucleotidyltransferase Research Article |
| Zdroj: | Biochemical Journal. 310:249-253 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj3100249 |
| Popis: | Inactivation of ribosomes by gelonin, a ribosome-inactivating protein with RNA N-glycosidase activity on 28 S rRNA, requires macromolecular cofactors present in post-ribosomal supernatants. One of these cofactors has been purified from a rat liver extract and identified as an RNA about 70 nt long which in sequence analysis shows a high level of similarity with mammalian (bovine) tRNA(Trp). The pattern of the sequencing gel is consistent with the co-existence in the preparation of two 3′-immature tRNA(Trp) species, missing only A75, or both A75 and C74. In the presence of ATP, CTP and tRNA nucleotidyltransferase, the gelonin-stimulating RNA is a good acceptor of tryptophan. An oligodeoxynucleotide complementary to positions 55 to 72 of mammalian (bovine) tRNA(Trp) hybridizes with the gelonin-stimulating RNA as demonstrated by gel mobility shift and ribonuclease H digestion. The oligodeoxynucleotide-directed ribonuclease H treatment also abolishes the gelonin-promoting activity of crude preparations of RNA, giving strong evidence that the only active RNA is a tRNA(Trp)-like molecule. |
| Databáze: | OpenAIRE |
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