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DNA binding activity of the mammalian translation elongation complex: recognition of chromium- and
J F Wang1, B N Engelsberg, S W Johnson
1Department of Pathology, School of Dental Medicine, University of Pennsylvania, Philadelphia 19104-6002, USA.
Abstract:
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.