title: Periodicities designed in the tropomyosin sequence and structure define its functions.
abstract: 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.
authors.affiliation: Department of Pathology and Laboratory Medicine, Robert Wood Johnson Medical School, Piscataway, NJ, USA. baruabi@rwjms.rutgers.edu
authors.forename: Bipasha
authors.initials: B
authors.lastname: Barua
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D011485:Protein Binding; D017433:Protein Structure, Secondary; D014335:Tropomyosin / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D000199:Actins; D014335:Tropomyosin
keywords: actin filament; coiled coil; cytoskeleton; muscle regulation; tropomyosin