Key result
The periodic heptad repeat sequence and structural features of the tropomyosin molecule determine its universal functions in binding and regulating the actin filament.
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Design
Review
This review summarizes how the periodic sequence and structural features of tropomyosin determine its interaction with actin filaments and isoform-specific functions.
Tropomyosin is an actin binding protein that regulates actin filament dynamics and its interactions with actin binding proteins such as myosin, tropomodulin, formin, Arp2/3 and ADF-cofilin in most eukaryotic cells. Tropomyosin is the prototypical two-chained, α-helical coiled coil protein that associates end-to-end and binds to both sides of the actin filament. Each tropomyosin molecule spans four to seven actin monomers in the filament, depending on the size of the tropomyosin. Tropomyosins have a periodic heptad repeat sequence that is characteristic of coiled coil proteins as well as additional periodicities required for its interaction with the actin filament, where each periodic repeat interacts with one actin molecule. This review addresses the role of periodic features of the Tm molecule in carrying out its universal functions of binding to the actin filament and its regulation and the specific features that may determine the isoform specificity of tropomyosins.
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Bipasha Barua (2013) reported a review. The periodic heptad repeat sequence and structural features of the tropomyosin molecule determine its universal functions in binding and regulating the actin filament.
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