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Crosslinking of tRNAs by the carcinostatic agent dirhodium tetraacetate
1Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.
Journal of Biomolecular Structure & Dynamics
|December 1, 1984
Abstract:
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.