DNA binding activity of the mammalian translation elongation complex: recognition of chromium- and transplatin-damaged DNA
| Autor: | Jian Fei Wang, Harry Rozmiarek, Steven W. Johnson, Paul C. Billings, Charlotte M. Witmer, Beatrice N. Engelsberg, William C. Merrick |
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| Rok vydání: | 1997 |
| Předmět: |
Chromium
HMG-box DNA damage Health Toxicology and Mutagenesis Molecular Sequence Data Biology Toxicology Ligands chemistry.chemical_compound DNA Adducts Tumor Cells Cultured Animals Humans Amino Acid Sequence Replication protein A chemistry.chemical_classification Ovarian Neoplasms DNA ligase DNA clamp Carcinoma General Medicine Peptide Elongation Factors Neoplasm Proteins Elongation factor DNA binding site DNA-Binding Proteins Cross-Linking Reagents chemistry Biochemistry Female Cisplatin DNA DNA Damage |
| Zdroj: | Archives of toxicology. 71(7) |
| ISSN: | 0340-5761 |
| Popis: | The elongation factor complex, EF-1H, serves an essential function in protein biosynthesis in eukaryotic cells, although the role of EF-1H in other physiological processes is unknown. In this report, we demonstrate that three components of EF-1H (EF-1 beta, EF-1 delta, EF-1 gamma) bind to DNA modified with chromium (Cr), a potent DNA-damaging agent and an established human carcinogen. The EF-1H complex also binds to transplatin modified DNA but not to cisplatin-modified DNA. These results demonstrate that the EF-1H complex has functional DNA binding activity and is capable of recognizing the distortions in DNA structure resulting from the covalent binding of Cr and transplatin to DNA. |
| Databáze: | OpenAIRE |
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