Efficient translation and polyribosome binding of 125I-labelled rabbit globin messenger ribonucleoprotein
| Autor: | P.D. Butcher, H.R.V. Arnstein |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Translation
Reticulocytes Lysis Biophysics Cycloheximide Biology Radioiodination Biochemistry Iodine Radioisotopes chemistry.chemical_compound Methionine Reticulocyte Structural Biology Labelling Genetics medicine Animals Moiety RNA Messenger Globin Molecular Biology fungi Translation (biology) Cell Biology Globins Polyribosome binding Messenger RNP Nucleoproteins medicine.anatomical_structure Ribonucleoproteins chemistry Isotope Labeling Polyribosomes Protein Biosynthesis Rabbits Messenger ribonucleoprotein |
| Zdroj: | FEBS Letters. (1):119-124 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(83)80130-6 |
| Popis: | Rabbit polyribosomal globin messenger ribonucleoprotein (mRNP) was labelled under mild conditions, using 125I and Iodogen, in the protein moiety so that the fate of mRNA-associated proteins could be followed during translation. 125I-mRNP was shown to retain functional activity in the nuclease-treated reticulocyte lysate translation system under optimal labelling conditions. Polyribosome binding of 125I-mRNP and its sensitivity to cycloheximide indicated a functional- and translation-dependent binding of mRNP proteins. The results constitute a successful and direct approach to the study of mRNA-associated proteins in translational control. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|