Evidence That Glutathione Peroxidase RNA and Manganese Superoxide Dismutase RNA Bind the Same Protein
| Autor: | Linda Biadasz Clerch, Angelique E Wright, David J. Chung |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Untranslated region
Biophysics Plasma protein binding Binding Competitive Biochemistry RNA Complementary chemistry.chemical_compound Animals RNA Messenger Lung Molecular Biology chemistry.chemical_classification Glutathione Peroxidase Messenger RNA Binding Sites Selenocysteine biology Superoxide Dismutase Glutathione peroxidase RNA-Binding Proteins RNA RNA Probes Cell Biology Molecular biology Stop codon Rats Isoenzymes chemistry Polyribosomes biology.protein Protein G Oxidation-Reduction |
| Zdroj: | Biochemical and Biophysical Research Communications. 222:590-594 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1996.0788 |
| Popis: | Rat lung extract contains protein that binds to a cis element in the 3′ untranslated region of glutathione peroxidase (GPx) mRNA; this region is located 200 bases downstream of the stop codon and 77 bases downstream of the selenocysteine insertion sequence. GPx mRNA-binding protein (GPx-BP) has the following characteristics in common with Mn superoxide dismutase mRNA-binding protein (MnSOD-BP): 1. RNA-binding activity is redox-sensitive; free sulfhydryl groups on the protein are required for binding. 2. RNA-binding activity is enriched in a 130,000 × g supernatant fraction and is inhibited by RNA in the polysomal fraction. 3. The MnSOD and GPx cis elements compete with each other for protein binding. 4. UV crosslinking studies with each probe reveal a [ 32 P]-labeled protein of the same apparent molecular mass, 56 kDa. These observations provide evidence that MnSOD and GPx RNAs bind the same protein. |
| Databáze: | OpenAIRE |
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