Crosslinking of tRNAs by the carcinostatic agent dirhodium tetraacetate.

A crystalline complex of yeast tRNA(phe) and dirhodium tetraacetate (DRTA) was prepared and its X-ray structure determined. The bifunctional DRTA forms an intermolecular cross-link between the N(1) position of adenine A36 in the anticodon triplet and possibly a ribose hydroxyl group of residue A76 at the 3' terminus of a symmetry related tRNA molecule. The rhodium complex apparently shows a preference for binding to the N(1) position of adenine in a single strand region of the tRNA molecule.