NDLI: Head-Head Interactions of Resting Myosin Crossbridges in Intact Frog Skeletal Muscles, Revealed by Synchrotron X-Ray Fiber Diffraction

Content Provider	PubMed Central
Author	Oshima, Kanji Sugimoto, Yasunobu Irving, Thomas C. Wakabayashi, Katsuzo
Editor	Pastore, Annalisa
Copyright Year	2012
Abstract	The intensities of the myosin-based layer lines in the x-ray diffraction patterns from live resting frog skeletal muscles with full thick-thin filament overlap from which partial lattice sampling effects had been removed were analyzed to elucidate the configurations of myosin crossbridges around the thick filament backbone to nanometer resolution. The repeat of myosin binding protein C (C-protein) molecules on the thick filaments was determined to be 45.33 nm, slightly longer than that of myosin crossbridges. With the inclusion of structural information for C-proteins and a pre-powerstroke head shape, modeling in terms of a mixed population of regular and perturbed regions of myosin crown repeats along the filament revealed that the myosin filament had azimuthal perturbations of crossbridges in addition to axial perturbations in the perturbed region, producing pseudo-six-fold rotational symmetry in the structure projected down the filament axis. Myosin crossbridges had a different organization about the filament axis in each of the regular and perturbed regions. In the regular region that lacks C-proteins, there were inter-molecular interactions between the myosin heads in axially adjacent crown levels. In the perturbed region that contains C-proteins, in addition to inter-molecular interactions between the myosin heads in the closest adjacent crown levels, there were also intra-molecular interactions between the paired heads on the same crown level. Common features of the interactions in both regions were interactions between a portion of the 50-kDa-domain and part of the converter domain of the myosin heads, similar to those found in the phosphorylation-regulated invertebrate myosin. These interactions are primarily electrostatic and the converter domain is responsible for the head-head interactions. Thus multiple head-head interactions of myosin crossbridges also characterize the switched-off state and have an important role in the regulation or other functions of myosin in thin filament-regulated muscles as well as in the thick filament-regulated muscles.
Related Links	http://dx.doi.org/10.1371/journal.pone.0052421
Starting Page	52421
File Format	PDF
ISSN	19326203
e-ISSN	19326203
Journal	PLoS ONE
Issue Number	12
Volume Number	7
Language	English
Publisher	Public Library of Science
Publisher Date	2012-12-20
Access Restriction	Open
Rights Holder	Public Library of Science
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Correction: Head-Head Interactions of Resting Myosin Crossbridges in Intact Frog Skeletal Muscles, Revealed by Synchrotron X-Ray Fiber Diffraction

X-RAY DIFFRACTION STUDIES ON FROG MUSCLES

Structural changes in the myosin filament and cross-bridges during active force development in single intact frog muscle fibres: stiffness and X-ray diffraction measurements

X-ray diffraction observations of chemically skinned frog skeletal muscle processed by an improved method.

Studies of the diffuse x-ray scattering from contracting frog skeletal muscles.

X-ray evidence that in contracting live frog muscles there exist two distinct populations of myosin heads.

Synchrotron x-ray diffraction studies of actin structure during polymerization.

Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction.

Cross-bridge conformation as revealed by x-ray diffraction studies on insect flight muscles with ATP analogues.

Head-Head Interactions of Resting Myosin Crossbridges in Intact Frog Skeletal Muscles, Revealed by Synchrotron X-Ray Fiber Diffraction

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Correction: Head-Head Interactions of Resting Myosin Crossbridges in Intact Frog Skeletal Muscles, Revealed by Synchrotron X-Ray Fiber Diffraction

X-RAY DIFFRACTION STUDIES ON FROG MUSCLES

Structural changes in the myosin filament and cross-bridges during active force development in single intact frog muscle fibres: stiffness and X-ray diffraction measurements

X-ray diffraction observations of chemically skinned frog skeletal muscle processed by an improved method.

Studies of the diffuse x-ray scattering from contracting frog skeletal muscles.

X-ray evidence that in contracting live frog muscles there exist two distinct populations of myosin heads.

Synchrotron x-ray diffraction studies of actin structure during polymerization.

Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffraction.

Cross-bridge conformation as revealed by x-ray diffraction studies on insect flight muscles with ATP analogues.

Head-Head Interactions of Resting Myosin Crossbridges in Intact Frog Skeletal Muscles, Revealed by Synchrotron X-Ray Fiber Diffraction