ArticleBiophysical journal2001
Coiled-coil unwinding at the smooth muscle myosin head-rod junction is required for optimal mechanical performance.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Engineering filamentous myosins for optical control of contractility.bioRxiv : the preprint server for biology · 2025Article
- Double-headed binding of myosin II to F-actin shows the effect of strain on head structure.Journal of structural biology · 2023Article
- The myosin II coiled-coil domain atomic structure in its native environment.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- A conformational transition in the myosin VI converter contributes to the variable step size.Biophysical journal · 2011Article
- Common structural motifs for the regulation of divergent class II myosins.The Journal of biological chemistry · 2010Review
- The elastic properties of the structurally characterized myosin II S2 subdomain: a molecular dynamics and normal mode analysis.Biophysical journal · 2008Article
- An unstable head-rod junction may promote folding into the compact off-state conformation of regulated myosins.Journal of molecular biology · 2008Article
- 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
- Lever arms and necks: a common mechanistic theme across the myosin superfamily.Journal of muscle research and cell motility · 2004Review
- A mutant heterodimeric myosin with one inactive head generates maximal displacement.The Journal of cell biology · 2003Article
- The kinetic properties of smooth muscle: how a little extra weight makes myosin faster.Journal of muscle research and cell motility · 2003Review
- Holding two heads together: stability of the myosin II rod measured by resonance energy transfer between the heads.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
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Authors and funding
4 authors.
Funding
Abstract
Myosin II has two heads that are joined together by an alpha-helical coiled-coil rod, which can separate in the region adjacent to the head-rod junction (Trybus, K. M. 1994. J. Biol. Chem. 269:20819-20822). To test whether this flexibility at the head-rod junction is important for the mechanical performance of myosin, we used the optical trap to measure the unitary displacements of heavy meromyosin constructs in which a stable coiled-coil sequence derived from the leucine zipper was introduced into the myosin rod. The zipper was positioned either immediately after the heads (0-hep zip) or following 15 heptads of native sequence (15-hep zip). The unitary displacement (d) decreased from d = 9.7 +/- 0.6 nm for wild-type heavy meromyosin (WT HMM) to d = 0.1 +/- 0.3 nm for the 0-hep zip construct (mean +/- SE). Native values were restored in the 15-hep zip construct (d = 7.5 +/- 0.7 nm). We conclude that flexibility at the myosin head-rod junction, which is provided by an unstable coiled-coil region, is essential for optimal mechanical performance.
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