This basic science study demonstrates a new interthiol crosslinking mechanism that traps nucleotides at the ATPase site of myosin subfragment 1.
No immediate clinical implications for myosin-targeted therapies; leaves open mechanistic studies of ATPase regulation in muscle.
When myosin subfragment 1 derivatives in which the reactive sulfhydryl SH1 has been blocked react with N,N'-p-phenylenedimaleimide or 5,5'-dithiobis(2-nitrobenzoic acid), the reactive sulfhydryl group SH2 of the 20-kDa domain is crosslinked with a thiol of the 50-kDa domain of the heavy chain. The crosslink induces the stable trapping of a significant amount of Mg2+-nucleotide in the ATPase site.
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Chaussepied et al. (1986) studied this question.
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