This basic science study demonstrates that the acidic residues at the N-terminus of actin are essential for myosin binding.
No immediate clinical implications; leaves open the role of actin N-terminus in mammalian muscle function.
Three N-terminal double mutants of beta-actin expressed in the yeast Saccharomyces cerevisiae have been characterized with respect to DNase-I interaction, N-terminal post-translational modification, polymerizability and myosin subfragment-1 binding. The results strongly support earlier suggestions that the acidic residues at the N-terminus of actin are part of the myosin-binding site, while they seem to be of no importance for the other aspects of actin biochemistry tested. The suitability of this expression system for production of recombinant actin in general is discussed.
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Aspenström et al. (1991) studied this question.
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