Contrary to previous reports, tropomyosin exists in an equilibrium between monomer, dimer, and tetramer, which has implications for the assembly of the tropomyosin-actin complex.
Challenges prior reports of stable oligomers; leaves open how equilibrium states regulate actin assembly in vivo.
It has recently been reported that tropomyosin exists exclusively as a dimer in physiological salt conditions. It is shown in the present work using analytical ultracentrifugation that, on the contrary, tropomyosin is in equilibrium between monomer, dimer and tetramer with a weak tendency to dimerize and tetramerize. Such a finding has consequences for the assembly of the tropomyosin-actin complex.
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Stafford et al. (2012) studied this question.
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