Structure and Function of the Iron-Responsive Element from Human Ferritin L Chain mRNA
| Autor: | Wolfgang Mikulits, Ernst W. Müllner, Thomas Sauer, Anthony A. Infante, Jose A. Garcia-Sanz |
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| Rok vydání: | 1997 |
| Předmět: |
Iron-Sulfur Proteins
DNA Complementary Iron T-Lymphocytes Protein subunit Molecular Sequence Data Biophysics Biology Biochemistry Sequence Homology Nucleic Acid Polysome Complementary DNA Humans RNA Messenger Cloning Molecular Molecular Biology Regulation of gene expression Messenger RNA Base Sequence cDNA library fungi Iron-Regulatory Proteins RNA-Binding Proteins Cell Biology Ferritin L-chain Blotting Northern Molecular biology Ferritin Ferritins biology.protein Nucleic Acid Conformation Electrophoresis Polyacrylamide Gel DNA Probes HeLa Cells |
| Zdroj: | Biochemical and Biophysical Research Communications. 235:212-216 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1997.6647 |
| Popis: | We report the cloning and functional characterization of the iron responsive element (IRE) of human ferritin light (L) chain mRNA from a cDNA library of primary human T lymphocytes. Comparison of this palindromic cDNA element to the IRE predicted from the reported genomic sequence revealed significant differences, resulting in a stem-loop structure with lower stability than the IRE of the heavy (H) chain mRNA. Nevertheless, the L subunit IRE mediated efficient binding of the iron regulatory protein (IRP) in a manner comparable to that of human ferritin H chain mRNAin vitro.In accordance with previous observations on H form transcripts, thecis-acting regulatory IRE motif of human ferritin L chain mRNA was capable of repressing translation under iron deprivation but permitted mobilization of the transcripts into polysomes following iron repletionin vivo. |
| Databáze: | OpenAIRE |
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