Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle

Yanagida, Toshio; Arata, Toshiaki; Oosawa, Fumio

doi:10.1038/316366a0

Cited by 252 publications

(126 citation statements)

References 29 publications

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“…Increased myofilament spacing reduces force production in these muscles, and this increased spacing likely induces a small but significant reduction in force production (April and Maughan, 1986). Readers should discount an early report that crab actomyosin has a 60 nm working stroke (Yanagida et al, 1985), which resulted from a failure to appreciate the effects on actomyosin sliding velocity measurements of still attached myosin heads that had finished their power stroke ('drag' attachments) (Brenner, 2006). X-ray diffraction and electron microscopy of crayfish and crab muscle in rigor and AMPPNP agrees well with asynchronous flight muscle data.…”

Section: Other Groups-actomyosinmentioning

confidence: 99%

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

128

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This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

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Section: Other Groups-actomyosinmentioning

confidence: 99%

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

128

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“…An experiment to investigate the in¯ux±ef¯ux relation in a sliding machine composed of myosin and actin ®laments was ®rst attempted by Yanagida et al in 1985, 30 years after the proposal of`sliding' as the mechanism of muscle contraction (Huxley & Hanson 1954;Huxley & Niedergerke 1954;Yanagida et al 1985).…”

Section: The Sliding Machinementioning

confidence: 99%

“…However, the situation was not so simple. The experiment by Yanagida et al in 1985 gave an unexpected resultÐlong distance sliding by hydrolysis of one ATP molecule. This result was not readily accepted and its signi®cance was not fully understood.…”

Section: The Unit Machine Of Slidingmentioning

confidence: 99%

The loose coupling mechanism in molecular machines of living cells

Oosawa

2000

Genes to Cells

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Living cells have molecular machines for free energy conversion, for example, sliding machines in muscle and other cells,¯agellar motors in bacteria, and various ion pumps in cell membranes. They are constructed from protein molecules and work in the nm (nanometer), pN (piconewton) and ms (millisecond) ranges, without inertia. In 1980s, a question was raised of whether the input±output or in¯ux±ef¯ux coupling in these molecular machines is tight or loose, and an idea of loose coupling was proposed. Recently, the long-distance multistep sliding of a single myosin head on an actin ®lament, coupled with the hydrolysis of one ATP molecule, was observed by Yanagida's group using highly developed techniques of optical microscopy and micromanipulation. This gave direct evidence for the loose coupling between the chemical reaction and the mechanical event in the sliding machine. In this review, I will brie¯y describe a historical overview of the input±output problem in the molecular machines of living cells. Input±output in molecular machinesConsider a series of solid gears. The ratio of the angle of rotation of a gear in the input to the angle of rotation of another gear in the output is constant and independent of the speed of rotation or the torque for rotation. In such a way, are the input and output or in¯ux and ef¯ux in molecular machines of living cells tightly coupled? Does one chemical reaction in the input always generate a unit mechanical movement in the output?The molecular machines are very small, so that the input free energy is not much larger than the energy of thermal noise. Nevertheless, the machine is neither cooled nor isolated, but works at room temperature in water. The structural units of the machine, the protein molecules, are not rigid, but have thermal¯uctuation. The energy exchange among these units and their environment may be positively involved in the process of free energy conversion. The relation between input and output in the machine would not be straightforward. Intermediate processes in the machine would make the in¯ux±ef¯ux coupling loose. It is very likely that living cells invented the loose coupling mechanism in order to give an ef®cient conversion of small free energy in thermal noise.To understand the working principle of molecular machines, it is important to know, ®rst of all, their function. We have to de®ne their input and output, or in¯ux and ef¯ux, and carry out quantitative investigations on the relation between them under various conditions.

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“…That is interactions between actin and myosin molecules (Huxley and Niedergerke, 1954;Huxley and Hanson, 1954;Huxley, 1969;Huxley and Simmons, 1971;Yanagida et al, 1985;Yanagida, 1990;Harada et al, 1990;Pollack, 1996). Fluorescent microscope technique in the framework of in vitro motility assay enables one to directly observe the sliding movement of actin filaments on HMMs fixed on the glass surface (Yanagida et al, 1984;Honda et al, 1986;Kron and Spudich, 1986;Harada et al, 1987;deBeer et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Up-and-down movement of a sliding actin filament in the in vitro motility assay

2011

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a b s t r a c tWe observed a three-dimensional up-and-down movement of an actin filament sliding on heavy meromyosin (HMM) molecules in an in vitro motility assay. The up-and-down movement occurred along the direction perpendicular to the planar glass plane on which the filament demonstrated a sliding movement. The height length of the up-and-down movement was measured by monitoring the extent of diminishing fluorescent emission from the marker attached to the filament in the evanescent field of attenuation. The height lengths whose distribution exhibits a local maximum were found around the two values, 150 nm and 90 nm, separately. This undulating three-dimensional movement of an actin filament suggests that the interactions between myosin (HMM) molecules and the actin filament may temporally be modulated during its sliding movement.

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Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle

Cited by 252 publications

References 29 publications

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

The loose coupling mechanism in molecular machines of living cells

Up-and-down movement of a sliding actin filament in the in vitro motility assay

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