Electron microscopic evidence for the myosin head lever arm mechanism in hydrated myosin filaments using the gas environmental chamber

Minoda, Hiroki; Okabe, Tatsuhiro; Inayoshi, Yuhri; Miyakawa, Takuya; Miyauchi, Yumiko; Tanokura, Masaru; Katayama, Eisaku; Wakabayashi, T.; Akimoto, Tsuyoshi; Sugi, Haruo

doi:10.1016/j.bbrc.2011.01.087

Cited by 23 publications

(19 citation statements)

References 13 publications

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“…Laser power00.1 μW (Minton 2001) because muscle is an exceptionally dense environment (Bagshaw 1982). Therefore, kinetics obtained here are different than those obtained before in in vitro in solution experiments (Jacobs et al 2011), by X-ray (Brown et al 2011;Minoda et al 2011), by AFM (Kodera et al 2010), by electron tomography (Wu et al 2010), by laser trap (Sleep et al 2006), and in single molecule experiments in myosin II (Warshaw et al 1998;Quinlan et al 2005), myosin V (Forkey et al 2003), myosin VI (Reifenberger et al 2009;Spudich 2008;Sun et al 2007), and in myosin X (Sun et al 2010). …”

Section: Resultsmentioning

confidence: 67%

Mesoscopic analysis of motion and conformation of cross-bridges

2012

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The orientation of a cross-bridge is widely used as a parameter in determining the state of muscle. The conventional measurements of orientation, such as that made by wide-field fluorescence microscopy, electron paramagnetic resonance (EPR) or X-ray diffraction or scattering, report the average orientation of 10 12 -10 9 myosin cross-bridges. Under conditions where all the cross-bridges are immobile and assume the same orientation, for example in normal skeletal muscle in rigor, it is possible to determine the average orientation from such global measurements. But in actively contracting muscle, where a parameter indicating orientation fluctuates in time, the measurements of the average value provide no information about cross-bridge kinetics. To avoid problems associated with averaging information from trillions of cross-bridges, it is necessary to decrease the number of observed cross-bridges to a mesoscopic value (i.e. the value affected by fluctuations around the average). In such mesoscopic regimes, the averaging of the signal is minimal and dynamic behavior can be examined in great detail. Examples of mesoscopic analysis on skeletal and cardiac muscle are provided.

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Section: Resultsmentioning

confidence: 67%

Mesoscopic analysis of motion and conformation of cross-bridges

2012

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“…As a matter of fact, we have already succeeded to study the myosin head power stroke in hydrated myosin filaments in the presence of actin filaments. A preliminary report of this work has appeared (Minoda et al,2011).…”

Section: Resultsmentioning

confidence: 99%

“…The ATP-induced movement at three different parts within individual myosin heads was recorded using myosin filaments with myosin heads position-marked with antibodies 1, 2 or 3 and 3' by the method previously described. (Minoda et al,2011). Fig.…”

Section: Electron Microscopic Evidence For Lever Arm Mechanism Of Myomentioning

confidence: 99%

“…(Minoda et al,2011). In the absence of actin filaments, the myosin head is initially thought to be in the post-power stroke configuration (solid line in D), and on binding with applied ATP it changes its conformation to reach the post-power stroke configuration with bound ATP hydrolysis products( Pi and ADP) (broken line in D). During this recovery stroke, the myosin head lever arm domain rotates not only around the converter domain, but also around the boundary between the lever arm domain and myosin S2, connecting the myosin head to myosin filament backbone.…”

Section: Electron Microscopic Evidence For Lever Arm Mechanism Of Myomentioning

confidence: 99%

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The Gas Environmental Chamber as a Powerful Tool to Study Structural Changes of Living Muscle Thick Filaments Coupled with ATP Hydrolysis

Sugi¹,

Minoda²,

Miyakawa³

et al. 2012

Current Basic and Pathological Approaches to the Function of Muscle Cells and Tissues - From Molecules to Humans

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“…Also using the gas environmental chamber, we could record ATP-induced movement at three different parts within individual S-1 heads with three different site-directed antibodies; antibody 1, antibody 2 to reactive lysine residue (RLR) located close to the COD, and antibody 3 to two peptides in the regulatory light chain in the LD (Fig.5) [14]. The results obtained are summarized in Fig.11.…”

Section: Evidence Against the Essential Role Of The Myosin Head Convementioning

confidence: 99%

Evidence for the Essential Role of Myosin Head Lever Arm Domain and Myosin Subfragment-2 in Muscle Contraction

Sugi¹,

Kobayashi²,

Tsuchiya³

et al. 2012

Skeletal Muscle - From Myogenesis to Clinical Relations

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Electron microscopic evidence for the myosin head lever arm mechanism in hydrated myosin filaments using the gas environmental chamber

Cited by 23 publications

References 13 publications

Mesoscopic analysis of motion and conformation of cross-bridges

Mesoscopic analysis of motion and conformation of cross-bridges

The Gas Environmental Chamber as a Powerful Tool to Study Structural Changes of Living Muscle Thick Filaments Coupled with ATP Hydrolysis

Evidence for the Essential Role of Myosin Head Lever Arm Domain and Myosin Subfragment-2 in Muscle Contraction

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