Interaction of tropomyosin with myelin basic protein and its effect on the ATPase activity of actomyosin.
Myelin basic protein (MBP) binds to both skeletal muscle and brain tropomyosin resulting in the formation of paracrystalline tactoids in the absence of divalent cations and at neutral pH. Both types of tropomyosin reduce the inhibition of the ATPase activity of actomyosin caused by MBP. On the other hand, MBP alters the effect of both brain and skeletal muscle tropomyosins on the actomyosin ATPase, even though MBP and tropomyosin bind independently to actin. We conclude that MBP cannot substitute for troponin I in the regulation of the action of tropomyosin on actin.
D000205:Actomyosin / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D066298:In Vitro Techniques; D004676:Myelin Basic Protein / Q000378:metabolism*; D014335:Tropomyosin / Q000378:metabolism*
D004676:Myelin Basic Protein; D014335:Tropomyosin; D000205:Actomyosin; D000251:Adenosine Triphosphatases