Mutations at the amino-terminus of beta-actin specifically alter its interaction with myosin without affecting polymerization or tropomyosin binding.
Does not inform clinical care; leaves open whether beta-actin N-terminal residues modulate myosin function in human disease models.
Neutral or charge-shifting mutagenesis of beta-actin at positions 3 and 4 strongly influenced the actomyosin interaction under non-rigor conditions. The polymerization behaviour and tropomyosin binding properties on the other hand remained unaffected.
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Aspenström et al. (1992) studied this question.
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