A functional interaction between methionyl-transfer RNA hydrolase and a transfer RNA binding factor
| Autor: | Boyd Hardesty, J.M. Cimadevilla, J. Morrisey |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Reticulocytes
Sodium chemistry.chemical_element Biology Sulfur Radioisotopes Ribosome Amino Acyl-tRNA Synthetases Methionine RNA Transfer Reticulocyte Structural Biology Hydrolase medicine Animals Magnesium Carbon Radioisotopes Peptide Chain Initiation Translational Molecular Biology Binding Sites Hydrolysis Esterases Temperature Substrate (chemistry) Ribosomal RNA TRNA binding medicine.anatomical_structure chemistry Biochemistry Transfer RNA Rabbits Ribosomes |
| Zdroj: | Journal of Molecular Biology. 83:437-446 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/0022-2836(74)90505-1 |
| Popis: | Met-tRNA f bound at low Mg ion concentrations to rabbit reticulocyte 40 S ribosomal subunits in the presence of ApUpG and a eukaryotic tRNA binding factor serves readily as a substrate for a Met-tRNA hydrolase from rabbit reticulocytes. This hydrolysis occurs rapidly at 0 °C, appears to be specific for Met-tRNA f , and is not inhibited by 60 S ribosomal subunits. These reactions may be responsible for the accumulation of deacylated tRNA f Met observed in ribosomes isolated from sodium fluoride-treated cells. |
| Databáze: | OpenAIRE |
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