A DNA-binding antitumor antibiotic binds to spectrin.

Aureolic acid group of antibiotics inhibit transcription by reversible binding to DNA in presence of divalent magnesium. We for the first time report binding of the one of such antitumor antibiotic, mithramycin (MTR), to the major protein component of erythrocyte cytoskeleton, spectrin. A reasonably high apparent dissociation constant was estimated to be 1.5 microM. The binding of mithramycin in the absence of any divalent cation to the large cytoskeletal protein led to quenching in the tryptophan fluorescence of the protein. Stern-Volmer quenching of the tryptophan residues by acrylamide revealed conformational change in the MTR-bound spectrin. This preliminary study might be useful in understanding other possible sites of actions after translocation.