The internal crosslinking of the S1 heavy chain from smooth muscle probed by dibromobimane.

The reaction of the crosslinker dibromobimane has recently revealed a functionally important internal loop structure within the skeletal myosin S1 heavy chain where Cys-522 of the 50K domain and Cys-707 (SH1) of the 20K region are spatially juxtaposed. Here we have studied the possible relevance of this topological feature to the architecture and transducing activity of the myosin head in general, by extending the dibromobimane modification to smooth muscle myosin. Treatment of chicken gizzard myosin S1 with dibromobimane resulted in intramolecular crosslinking between the C-terminal 25K and central 50K segments of the S1 heavy chain. The data suggest a conservation at the 50K-25K interface of smooth muscle S1 heavy chain and the importance of the neighboring SH1 region, whose conformation may play an important role in energy transduction by the myosin head.