Movement and force produced by a single myosin head
@article{Molloy1995MovementAF, title={Movement and force produced by a single myosin head}, author={Justin E. Molloy and Julie E. Burns and John Kendrick‐Jones and Richard T. Tregear and David C. S. White}, journal={Nature}, year={1995}, volume={378}, pages={209-212} }
MUSCLE contraction is driven by the cyclical interaction of myosin with actin, coupled to the breakdown of ATP. Studies of the interaction of filamentous myosin1 and of a double-headed proteolytic fragment, heavy meromyosin (HMM)2,3, with actin have demonstrated discrete mechanical events, arising from stochastic interaction of single myosin molecules with actin. Here we show, using an optical-tweezers transducer2,4, that a single myosin subfragment-1 (S1), which is a single myosin head, can…
587 Citations
The motor protein myosin-I produces its working stroke in two steps
- BiologyNature
- 1999
The slower kinetics of myosin-I have allowed us to observe the separate mechanical states that contribute to its working stroke, and an optical-tweezers transducer is used to measure the mechanical transitions made by a single myOSin head while it is attached to actin.
Two independent mechanical events in the interaction cycle of skeletal muscle myosin with actin.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 2006
The finding of a second mechanical event in the working stroke of skeletal muscle myosin provides the molecular basis for a simple model of actomyosin interaction that can account for the variation, in different fiber types, of the rate of the cross-bridge cycle and provides a common scheme for the chemo-mechanical transduction within the myOSin family.
The size and the speed of the working stroke of muscle myosin and its dependence on the force
- BiologyThe Journal of physiology
- 2002
It is shown that with 150 μs force steps it is possible to separate the elastic response from the subsequent early rapid component of filament sliding due to the working stroke in the attached myosin heads, and determine how the size and the speed of the working strokes depend on the clamped force.
Mechanism of muscle contraction based on stochastic properties of single actomyosin motors observed in vitro
- BiologyBiophysics
- 2005
Computer simulations show that multiple cooperating heads undergoing stochastic steps generate a long (>60 nm) sliding distance per ATP between actin and myosin filaments, i.e., the movement is loosely coupled to the ATPase cycle as observed in muscle.
Two heads of myosin are better than one for generating force and motion.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1999
Measurements of unitary displacement and force produced by double-headed and single-headed smooth- and skeletal-muscle myosin suggest that muscle myosins require both heads to generate maximal force and motion.
Load-dependent kinetics of force production by smooth muscle myosin measured with optical tweezers
- BiologyNature Cell Biology
- 2003
A new technique based on optical tweezers to rapidly apply force to a single smooth muscle myosin crossbridge that produced movement in two phases that contribute 4 nm + 2 nm of displacement.
A single myosin head moves along an actin filament with regular steps of 5.3 nanometres
- Biology, ChemistryNature
- 1999
A new instrument is developed with which individual myosin subfragment-1 molecules are captured and directly manipulated using a scanning probe to resolve the individual mechanical events of force generation by actomyosin.
A model of stereocilia adaptation based on single molecule mechanical studies of myosin I.
- BiologyPhilosophical transactions of the Royal Society of London. Series B, Biological sciences
- 2004
A new model is proposed to explain the slow phase of sensory adaptation of the hair cells of the inner ear, consistent with the classical 'T2' behaviour of single muscle fibres.
Molecular model of muscle contraction.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 1999
The model indicates that when large numbers of myosin molecules act collectively, their chemical cycles can be synchronized, and that this leads to stepwise motion of the thin filament.
Single-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin.
- Biology, ChemistryProceedings of the National Academy of Sciences of the United States of America
- 2005
Data support the hypothesis that thin filament inhibition in the absence of Ca(2+) is largely achieved by modulating the rate of attachment and/or transition from the weakly to strongly bound state, as well as the investigations of single- and multiple-myosin molecules with regulated thin filaments.
References
SHOWING 1-10 OF 12 REFERENCES
Sliding movement of single actin filaments on one-headed myosin filaments
- BiologyNature
- 1987
The results show that cooperative interaction between the two heads of myosin is not essential for inducing the sliding movement of actin filaments.
Single-molecule analysis of the actomyosin motor using nano-manipulation.
- BiologyBiochemical and biophysical research communications
- 1994
The results suggested that an ATPase cycle produces one power stroke at high load and many ones at low load, similar to those deduced from noise analysis of force fluctuations caused by multiple molecules.
Myosin subfragment-1 is sufficient to move actin filaments in vitro
- BiologyNature
- 1987
That S1 is sufficient to cause sliding movement of actin filaments in vitro gives strong support to models of contraction that place the site of active movement in muscle within the myosin head.
Stepwise motion of an actin filament over a small number of heavy meromyosin molecules is revealed in an in vitro motility assay.
- Biology, ChemistryJournal of biochemistry
- 1994
In order to determine the relative motions of an actin filament and a myosin molecule upon hydrolysis of one ATP, an in vitro motility assay, in which individual actin filaments slide over heavy…
Force measurements by micromanipulation of a single actin filament by glass needles
- BiologyNature
- 1988
The tensile strength of the F-actin–phalloidin complex is comparable with the average force exerted on a single thin filament in muscle fibres during isometric contraction and the myosin head (subfragment-1) can produce the same ATP-dependent force as intact myOSin.
Single myosin molecule mechanics: piconewton forces and nanometre steps
- Biology, PhysicsNature
- 1994
A new in vitro assay using a feedback enhanced laser trap system allows direct measurement of force and displacement that results from the interaction of a single myosin molecule with a single…
Direct measurement of stiffness of single actin filaments with and without tropomyosin by in vitro nanomanipulation.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1994
The results suggest that approximately 50% of the sarcomere compliance of active muscle is due to extensibility of the thin filaments.
Three-dimensional structure of myosin subfragment-1: a molecular motor.
- Chemistry, BiologyScience
- 1993
The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described, and this structure of a molecular motor was determined by single crystal x-ray diffraction.
Direct observation of kinesin stepping by optical trapping interferometry
- BiologyNature
- 1993
It is found that kinesin moves with 8-nm steps, similar to biological motors that move with regular steps.