Cotranslational heme binding to nascent globin chains
| Autor: | Igor A. Krasheninnikov, Anton A. Komar, Aigar Kommer, Alexander S. Spirin |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Protein Folding
Hemeprotein Reticulocytes Heme binding Biophysics Attachment Heme Biology Tritium Biochemistry chemistry.chemical_compound Reticulocyte Structural Biology Leucine hemic and lymphatic diseases Polysome Cotranslational folding Genetics medicine Centrifugation Density Gradient polycyclic compounds Animals Globin RNA Messenger Hemoglobin Molecular Biology Cell-Free System Cell Biology Globins medicine.anatomical_structure chemistry Puromycin Polyribosomes Protein Biosynthesis Nascent peptide Hemin Rabbits |
| Zdroj: | FEBS Letters. (1-3):261-263 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(93)81803-8 |
| Popis: | Globin synthesis in cell-free extracts of rabbit reticulocytes was carried out in the presence of 3H-labeled hemin. Sucrose gradient centrifugation analysis revealed [3H]hemin in the polyribosome fraction. The addition of puromycin resulted in the release of both [3H]hemin- and [14C]leucine-labeled polypeptide from the polyribosomes. The data suggest cotranslational folding of the globin molecule on the ribosome and cotranslational heme binding to the nascent globin chain. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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