Abstract
Tropomyosin is a dimer coiled-coil actin-binding protein. Adjacent tropomyosin molecules connect each other ‘head-to-tail’ via an overlap junction and form a continuous strand that winds around an actin filament and controls the actin–myosin interaction. High cooperativity of muscle contraction largely depends on tropomyosin characteristics. Here we summarise experimental evidence that local peculiarities of tropomyosin structure have long-range effects and determine functional properties of the strand, including changes in its bending stiffness and interaction with actin and myosin. Point mutations and posttranslational modifications help to probe the roles of the conserved ‘non-canonical’ residues, clusters of stabilising and destabilising core residues, and core gap in tropomyosin function. The data suggest that tropomyosin structural lability including a diversity of homo- and heterodimers of different isoforms provide a balance of stiffness, flexibility, and strength of interaction with partner sarcomere proteins necessary for fine-tuning of Ca2+ regulation in various types of striated muscles.
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Abbreviations
- Tpm:
-
Tropomyosin
- Tn:
-
Troponin
- F-actin:
-
Filamentous actin
- EM:
-
Electron microscopy
- NMR:
-
Nuclear magnetic resonance
- CD:
-
Circular dichroism
- DSC:
-
Differential scanning calorimetry
- MD:
-
Molecular dynamics
- DTNB:
-
5,5′-Dithiobis(2-nitrobenzoate)
- WT:
-
Wild type
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Acknowledgements
The work was supported by the research Grants 17-00-00066 (to A.T.), 17-00-00070 (to S.B.), and 17-00-00065 (to D.L.) of the collaboration Project 17-00-00071 and the research Grant 18-015-00252 (to G.K.) of the Russian Foundation for Basic Research; and State Program Projects AAAA-A16-116021110193-0 to (A.T.), AAAA-A18-118020590135-3 (to S.B.), and AAAA-A19-119010590010-3 (to D.L.).
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Kopylova, G.V., Matyushenko, A.M., Koubassova, N.A. et al. Functional outcomes of structural peculiarities of striated muscle tropomyosin. J Muscle Res Cell Motil 41, 55–70 (2020). https://doi.org/10.1007/s10974-019-09552-8
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DOI: https://doi.org/10.1007/s10974-019-09552-8