ArticleBiochemistry2012
In vitro formation and characterization of the skeletal muscle α·β tropomyosin heterodimers.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Temperature dependence of activation of thick and thin filaments in skeletal and cardiac muscles.Journal of muscle research and cell motility · 2026Review
- Actin Filament Pointed Ends: Assays for Regulation of Assembly and Disassembly by Tropomodulin and Tropomyosin.Cytoskeleton (Hoboken, N.J.) · 2025Article
- A Novel Variant inInternational journal of molecular sciences · 2023Article
- Structural and Functional Properties of Kappa Tropomyosin.International journal of molecular sciences · 2023Article
- Article
- Mutations Q93H and E97K inInternational journal of molecular sciences · 2021Article
- Visualizing the in vitro assembly of tropomyosin/actin filaments using TIRF microscopy.Biophysical reviews · 2020Review
- Functional outcomes of structural peculiarities of striated muscle tropomyosin.Journal of muscle research and cell motility · 2020Review
- Homologous tropomyosins from vertebrate and invertebrate: Recombinant calibrator proteins in functional biological assays for tropomyosin allergenicity assessment of novel animal foods.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2020Article
- Investigating the effects of tropomyosin mutations on its flexibility and interactions with filamentous actin using molecular dynamics simulation.Journal of muscle research and cell motility · 2016Article
- Mechanistic heterogeneity in contractile properties of α-tropomyosin (TPM1) mutants associated with inherited cardiomyopathies.The Journal of biological chemistry · 2015Article
- Using fluorescent myosin to directly visualize cooperative activation of thin filaments.The Journal of biological chemistry · 2015Article
- Polymorphism in tropomyosin structure and function.Journal of muscle research and cell motility · 2013Review
- α-Tropomyosin with a D175N or E180G mutation in only one chain differs from tropomyosin with mutations in both chains.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Tropomyosin (Tm) is a dimer made of two alpha helical chains associated into a parallel coiled-coil. In mammalian skeletal and cardiac muscle, the Tm is expressed from two separate genes to give the α- and β-Tm isoforms. These associate in vivo to form homo- (α(2)) and heterodimers (α·β) with little β(2) normally observed. The proportion of α(2) vs α·β varies across species and across muscle types from almost 100% α(2)- to 50% α·β-Tm. The ratio can also vary during development and in disease. The functional significance of the presence of these two isoforms has not been defined because it is difficult to isolate or purify the α·β dimer for functional studies. Here we report an effective method for purifying bacterially expressed Tm as α·β dimers using a cleavable N-terminal tag on one of the two chains. The same method can be used to isolate Tm dimers in which one chain carries a mutation. We go on to show that the α·β dimers differ in key properties (actin affinity, thermal stability) from either the α(2)- or β(2)-Tm. However, the ability to regulate myosin binding when combined with cardiac troponin appears unaffected.
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Registered trials
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