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  • Title: Thermal unfolding of various human non-muscle isoforms of tropomyosin.
    Author: Nefedova VV, Marchenko MA, Kleymenov SY, Datskevich PN, Levitsky DI, Matyushenko AM.
    Journal: Biochem Biophys Res Commun; 2019 Jun 30; 514(3):613-617. PubMed ID: 31072616.
    Abstract:
    Tropomyosin (Tpm) is an α-helical coiled-coil protein dimer, which forms a continuous head-to-tail polymer along the actin filament. In striated muscles, Tpm plays an important role in the Ca2+-dependent regulation of muscle contraction. However, little is known about functional and especially structural properties of the numerous non-muscle Tpm isoforms. In the present work, we have applied circular dichroism (CD) and differential scanning calorimetry (DSC) to investigate thermal unfolding and domain structure of various non-muscle human Tpm isoforms. These isoforms, the products of two different genes, TPM1 and TPM3, also significantly differ by alternatively spliced exons: N-terminal exons 1a2b or 1b, internal exons 6a or 6b, and C-terminal exons 9a, 9c or 9d. Our results clearly demonstrate that structural properties of various non-muscle Tpm isoforms can be quite different depending on the presence of different alternatively spliced exons in their genes. These data show for the first time a significant difference in the thermal unfolding between muscle and non-muscle Tpm isoforms and indicate that replacement of alternatively spliced exons alters the stability of certain domains in the Tpm molecule.
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