Abstract
It is known that ATP analogues such as 8-Br-ATP with bulky substitution at the eight position of the adenine ring predominantly assume the syn conformation with respect to the adenine-ribose bond. Previously we have demonstrated that 8-Br-ATP induces intrinsic trp fluorescence enhancement of smooth muscle myosin that reflect the formation of the M∗∗·ADP·Pi state. Moreover, the phosphorylated smooth muscle myosin supported actin translocation using 8-Br-ATP. Contrary, for skeletal muscle myosin, 8-Br-ATP induced neither trp fluorescence enhancement nor actin translocation. Kinesin is also ATP driven motor protein that has strikingly similar structure of motor domain to myosin. In the present study, interaction of kinesin with 8-Br-ATP has been examined. Interestingly, conventional kinesin supported microtubules translocation using 8-Br-ATP. This suggests conventional kinesin adopts the 8-Br-ATP in the normal conformation. However, the sliding velocity was approximately one-fifth of regular ATP. Moreover single molecular measurment using optical tweezers revealed that for kinesin, 8-Br-ATP induced nearly similar force generation with that of ATP. Myosin V is also processive motor protein like kinesin. Interaction of unconventional myosin V with 8-Br-ATP was also analyzed. Myosin V supported actin translocation using 8-Br-ATP. Currently, we are examining single molecular measurment of myosin V in the presence of 8-Br-ATP.
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