Tropomyosin movement on F-actin during muscle activation explained by energy landscapes
Muscle contraction is regulated by tropomyosin movement across the thin filament surface, which exposes or blocks myosin-binding sites on actin. Recent atomic structures of F-actin-tropomyosin have yielded the positions of tropomyosin on myosin-free and myosin-decorated actin. Here, the repositionin...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
8 January 2014
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| In: |
Archives of biochemistry and biophysics
Year: 2014, Volume: 545, Pages: 63-68 |
| ISSN: | 1096-0384 |
| DOI: | 10.1016/j.abb.2014.01.001 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.abb.2014.01.001 Verlag, lizenzpflichtig, Volltext: http://www.sciencedirect.com/science/article/pii/S0003986114000046 
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| Author Notes: | Marek Orzechowski, Jeffrey R. Moore, Stefan Fischer, William Lehman |
MARC
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| 520 | |a Muscle contraction is regulated by tropomyosin movement across the thin filament surface, which exposes or blocks myosin-binding sites on actin. Recent atomic structures of F-actin-tropomyosin have yielded the positions of tropomyosin on myosin-free and myosin-decorated actin. Here, the repositioning of α-tropomyosin between these locations on F-actin was systematically examined by optimizing the energy of the complex for a wide range of tropomyosin positions on F-actin. The resulting energy landscape provides a full-map of the F-actin surface preferred by tropomyosin, revealing a broad energy basin associated with the tropomyosin position that blocks myosin-binding. This is consistent with previously proposed low-energy oscillations of semi-rigid tropomyosin, necessary for shifting of tropomyosin following troponin-binding. In contrast, the landscape shows much less favorable energies when tropomyosin locates near its myosin-induced “open-state” position. This indicates that spontaneous movement of tropomyosin away from its energetic “ground-state” to the open-state is unlikely in absence of myosin. Instead, myosin-binding must drive tropomyosin toward the open-state to activate the thin filament. Additional energy landscapes were computed for disease-causing actin mutants that distort the topology of the actin-tropomyosin energy landscape, explaining their phenotypes. Thus, the computation of such energy landscapes offers a sensitive way to estimate the impact of mutations. | ||
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