ArticleThe Journal of biological chemistry2011
Conserved noncanonical residue Gly-126 confers instability to the middle part of the tropomyosin molecule.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- The unique biology of catch muscles: insights into structure, function, and robotics innovations.Frontiers in bioengineering and biotechnology · 2025Review
- Functional and Structural Properties of Cytoplasmic Tropomyosin Isoforms Tpm1.8 and Tpm1.9.International journal of molecular sciences · 2024Article
- Structural and Functional Peculiarities of Cytoplasmic Tropomyosin Isoforms, the Products ofInternational journal of molecular sciences · 2021Article
- Impact of A134 and E218 Amino Acid Residues of Tropomyosin on Its Flexibility and Function.International journal of molecular sciences · 2020Article
- Functional outcomes of structural peculiarities of striated muscle tropomyosin.Journal of muscle research and cell motility · 2020Review
- Structural and Dynamic Properties of Allergen and Non-Allergen Forms of Tropomyosin.Structure (London, England : 1993) · 2018Article
- The structural basis of alpha-tropomyosin linked (Asp230Asn) familial dilated cardiomyopathy.Journal of molecular and cellular cardiology · 2017Article
- Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin.Journal of muscle research and cell motility · 2017Article
- The Relaxation Properties of Myofibrils Are Compromised by Amino Acids that Stabilize α-Tropomyosin.Biophysical journal · 2017Article
- Stabilizing the central part of tropomyosin increases the bending stiffness of the thin filament.Biophysical journal · 2015Article
- Tropomyosin dynamics.Journal of muscle research and cell motility · 2014Review
- Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction.Acta naturae · 2013Article
- Conserved Asp-137 is important for both structure and regulatory functions of cardiac α-tropomyosin (α-TM) in a novel transgenic mouse model expressing α-TM-D137L.The Journal of biological chemistry · 2013Article
- Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin.Biochemistry · 2012Article
- Structural implications of conserved aspartate residues located in tropomyosin's coiled-coil core.Bioarchitecture · 2011Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tropomyosin (Tm) is a two-stranded α-helical coiled-coil protein with a well established role in regulation of actin cytoskeleton and muscle contraction. It is believed that many Tm functions are enabled by its flexibility whose nature has not been completely understood. We hypothesized that the well conserved non-canonical residue Gly-126 causes local destabilization of Tm. To test this, we substituted Gly-126 in skeletal muscle α-Tm either with an Ala residue, which should stabilize the Tm α-helix, or with an Arg residue, which is expected to stabilize both α-helix and coiled-coil structure of Tm. We have shown that both mutations dramatically reduce the rate of Tm proteolysis by trypsin at Asp-133. Differential scanning calorimetry was used for detailed investigation of thermal unfolding of the Tm mutants, both free in solution and bound to F-actin. It was shown that a significant part of wild type Tm unfolds in a non-cooperative manner at low temperature, and both mutations confer cooperativity to this part of the Tm molecule. The size of the flexible middle part of Tm is estimated to be 60-70 amino acid residues, about a quarter of the Tm molecule. Thus, our results show that flexibility is unevenly distributed in the Tm molecule and achieves the highest extent in its middle part. We conclude that the highly conserved Gly-126, acting in concert with the previously identified non-canonical Asp-137, destabilizes the middle part of Tm, resulting in a more flexible region that is important for Tm function.
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