ArticleProceedings of the National Academy of Sciences of the United States of America2002
Holding two heads together: stability of the myosin II rod measured by resonance energy transfer between the heads.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Research reviews on myosin head interactions with F-actin.Applied microscopy · 2024Review
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- Article
- Mechanism of force enhancement during stretching of skeletal muscle fibres investigated by high time-resolved stiffness measurements.Journal of muscle research and cell motility · 2013Article
- A conformational transition in the myosin VI converter contributes to the variable step size.Biophysical journal · 2011Article
- Myosin binding protein-C: a regulator of actomyosin interaction in striated muscle.Journal of biomedicine & biotechnology · 2011Review
- Fluorescence applications in molecular neurobiology.Neuron · 2010Review
- MG53 regulates membrane budding and exocytosis in muscle cells.The Journal of biological chemistry · 2009Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Article
- The elastic properties of the structurally characterized myosin II S2 subdomain: a molecular dynamics and normal mode analysis.Biophysical journal · 2008Article
- Load-dependent mechanism of nonmuscle myosin 2.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Orientation of the myosin light chain region by single molecule total internal reflection fluorescence polarization microscopy.Biophysical journal · 2005Article
- Progress in lanthanides as luminescent probes.Journal of fluorescence · 2005Review
- Activation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA.Biophysical journal · 2004Article
- Photocytotoxicity of the fluorescent nonsteroidal androgen receptor ligand TDPQ.Photochemistry and photobiologyArticle
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Authors and funding
4 authors.
Funding
Abstract
Myosin, similar to many molecular motors, is a two-headed dimer held together by a coiled-coiled rod. The stability of the coiled coil has implications for head-head interactions, force generation, and possibly regulation. Here we used two different resonance energy transfer techniques to measure the distances between probes placed in the regulatory light chain of each head of a skeletal heavy meromyosin, near the head-rod junction (positions 2, 73, and 94). Our results indicate that the rod largely does not uncoil when myosin is free in solution, and at least beyond the first heptad, the subfragment 2 rod remains relatively intact even under the relatively large strain of two-headed myosin (rigor) binding to actin. We infer that uncoiling of the rod likely does not play a role in myosin II motility. To keep the head-rod junction intact, a distortion must occur within the myosin heads. This distortion may lead to different orientations of the light-chain domains within the myosin dimer when both heads are attached to actin, which would explain previously puzzling observations and require reinterpretation of others. In addition, by comparing resonance energy transfer techniques sensitive to different dynamical time scales, we find that the N terminus of the regulatory light chain is highly flexible, with possible implications for regulation. An intact rod may be a general property of molecular motors, because a similar conclusion has been reached recently for kinesin, although whether the rod remains intact will depend on the relative stiffness of the coiled coil and the head in different motors.
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