DNA-BINDING ACTIVITY OF THE MAMMALIAN TRANSLATION ELONGATION COMPLEX - RECOGNITION OF CHROMIUM-DAMAGED AND TRANSPLATIN-DAMAGED DNA

The elongation factor complex, EF-1H, serves an essential function in protein biosynthesis in eukaryotic cells, although the role of EF-1H i n other physiological processes is unknown. In this report, we demonst rate that three components of EF-1H (EF-1 beta, EF-1 delta, and EF-1 g amma) bind to DNA modified with chromium (Cr), a potent DNA-damaging a gent 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 structur e resulting from the covalent binding of Cr and transplatin to DNA.