Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3' untranslated region
| Autor: | N. Standart, D.H. Ostareck, Bernd J. Thiele, A. Ostareck-Lederer |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1994 |
| Předmět: |
Untranslated region
Reticulocytes Molecular Sequence Data Down-Regulation RNA-binding protein Biology General Biochemistry Genetics and Molecular Biology Chromatography Affinity Reticulocyte medicine Protein biosynthesis Animals Arachidonate 15-Lipoxygenase RNA Messenger Molecular Biology Repetitive Sequences Nucleic Acid Messenger RNA Binding Sites General Immunology and Microbiology Base Sequence Three prime untranslated region General Neuroscience Intron RNA RNA-Binding Proteins Blood Proteins Molecular biology Introns medicine.anatomical_structure Oligodeoxyribonucleotides Protein Biosynthesis Rabbits Research Article |
| Popis: | During red blood cell differentiation, the mRNA encoding rabbit erythroid 15-lipoxygenase (LOX) is synthesized in the early stages of erythropoiesis, but is only activated for translation in peripheral reticulocytes. Erythroid LOX, which like other lipoxygenases catalyses the degradation of lipids, is unique in its ability to attack intact phospholipids and is the main factor responsible for the degradation of mitochondria during reticulocyte maturation. Strikingly, rabbit erythroid LOX mRNA has 10 tandem repeats of a slightly varied, pyrimidine-rich 19 nt motif in its 3'-untranslated region (3'-UTR). In this study we demonstrate, using gel retardation and UV-crosslinking assays, that this 3'-UTR segment specifically binds a 48 kDa reticulocyte protein. Furthermore, the interaction between the 3'-UTR LOX repeat motif and the 48 kDa protein, purified to homogeneity by specific RNA chromatography, is shown to be necessary and sufficient for specific translational repression of LOX as well as reporter mRNAs in vitro. To our knowledge this is the first case in which translation, presumably at the initiation step, is regulated by a defined protein-RNA interaction in the 3'-UTR. |
| Databáze: | OpenAIRE |
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