Tropomyosin diffusion over actin subunits facilitates thin filament assembly
Coiled-coil tropomyosin binds to consecutive actin-subunits along actin-containing thin filaments. Tropomyosin molecules then polymerize head-to-tail to form cables that wrap helically around the filaments. Little is known about the assembly process that leads to continuous, gap-free tropomyosin cab...
Gespeichert in:
| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
14 January 2016
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| In: |
Structural dynamics
Year: 2016, Jahrgang: 3, Heft: 1 |
| ISSN: | 2329-7778 |
| DOI: | 10.1063/1.4940223 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1063/1.4940223 Verlag, lizenzpflichtig, Volltext: https://aca.scitation.org/doi/10.1063/1.4940223 
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| Verfasserangaben: | Stefan Fischer, Michael J. Rynkiewicz, Jeffrey R. Moore, and William Lehman |
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| 520 | |a Coiled-coil tropomyosin binds to consecutive actin-subunits along actin-containing thin filaments. Tropomyosin molecules then polymerize head-to-tail to form cables that wrap helically around the filaments. Little is known about the assembly process that leads to continuous, gap-free tropomyosin cable formation. We propose that tropomyosin molecules diffuse over the actin-filament surface to connect head-to-tail to partners. This possibility is likely because (1) tropomyosin hovers loosely over the actin-filament, thus binding weakly to F-actin and (2) low energy-barriers provide tropomyosin freedom for 1D axial translation on F-actin. We consider that these unique features of the actin-tropomyosin interaction are the basis of tropomyosin cable formation. | ||
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