Mechanism of inhibition of relaxation by N-ethylmaleimide treatment of myosin.
It has remained unexplained why N-ethylmalaeimide (NEM) treatment of myosin can inhibit relaxation in actomyosin systems from rabbit skeletal muscle which appear to be regulated solely through tropomyosin and troponin. Since rigor complexes between (nucleotide-free) myosin and actin affect the tropinin-tropomyosin system, the possibility was explored that, as a result of NEM treatment, some of the myosin maintains rigor complexes with actin in the presence of ATP which might be responsible for inhibition of relaxation. Evidence is presented indicating that such a mechanism might account for the effects of NEM treatment. First, after exhaustive NEM treatment of heavy meromysin (HMM), acto-HMM complexes were no longer dissociated by ATP. Second, admixture of such NEM-treated, enzymatically inactive HMM or myosin to native regulated actomyosin or acto-HMM inhibited relaxation.
D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D005033:Ethylmaleimide / Q000494:pharmacology; D007460:Iodoacetamide; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D009218:Myosins / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D011817:Rabbits
D000199:Actins; D000251:Adenosine Triphosphatases; D009218:Myosins; D005033:Ethylmaleimide; D002118:Calcium; D007460:Iodoacetamide