Chemomechanical coupling of the forward and backward steps of single kinesin molecules

Nishiyama, Masayoshi; Higuchi, Hideo; Yanagida, Toshio

doi:10.1038/ncb857

Cited by 288 publications

(457 citation statements)

References 41 publications

Supporting

Mentioning

410

Contrasting

Order By: Relevance

“…In motor proteins, such as kinesin and myosin V, which walk on linear tracks, the forward step is associated with ATP hydrolysis, but the backward step is usually not caused by its reverse reaction (ATP synthesis). [19][20][21] Hence, our model as it is may not be applicable to these motor proteins.…”

Section: Modelmentioning

confidence: 99%

Enhanced Diffusion of Molecular Motors in the Presence of Adenosine Triphosphate and External Force

Shinagawa

Sasaki

2016

J. Phys. Soc. Jpn.

View full text Add to dashboard Cite

The diffusion of a molecular motor in the presence of a constant external force is considered on the basis of a simple theoretical model. The motor is represented by a Brownian particle moving in a series of parabolic potentials placed periodically on a line, and the potential is switched stochastically from one parabola to another by a chemical reaction, which corresponds to the hydrolysis or synthesis of adenosine triphosphate (ATP) in motor proteins. It is found that the diffusion coefficient as a function of the force exhibits peaks. The mechanism of this diffusion enhancement and the possibility of observing it in F 1 -ATPase, a biological rotary motor, are discussed.

show abstract

Section: Modelmentioning

confidence: 99%

Enhanced Diffusion of Molecular Motors in the Presence of Adenosine Triphosphate and External Force

Shinagawa

Sasaki

2016

J. Phys. Soc. Jpn.

View full text Add to dashboard Cite

show abstract

“…In most of the previous models, q was assumed constant [11,12]. However, the fact that energy is supplied only during the ATP hydrolysis process, taking about 7 ms [29,46], while walking one step takes about 30 ms, motivates us to use the above pulse-like energy supply. The pulse-like energy influx implies that the time for energy supply is much shorter than that for one-step walking.…”

Section: Model For Kinesin Motor On Microtubulementioning

confidence: 99%

“…One of the interesting observations is the backward moonwalking of kinesin [25,26,[28][29][30][31][32][33][34] under a backward load much larger than the stall force. There are reports that backward steps are related to ATP synthesis [33,35] or ATP hydrolysis [31][32][33][34].…”

mentioning

confidence: 99%

Walking motion of an overdamped active particle in a ratchet potential

2011

View full text Add to dashboard Cite

An active particle can convert its internal energy into mechanical work. We study a generalized energy-depot model of an overdamped active particle in a ratchet potential. Using well-known biological parameters for kinesin-1 and modeling ATP influx as a pulsed energy supply, we apply our model to the molecular motor system. We find that our simple model can capture the essential properties of the kinesin motor such as forward stepping, stalling, backward stepping, dependence on ATP concentration, and stall force. Our model might be quite universal in the sense that it is able to describe dynamics of various types of motors as long as realistic parameters for each motor species are adopted.

show abstract

“…The network calculations also provide very good descriptions for the experimental data in Refs. [16][17][18][19].…”

Section: Motor Dynamics For Processive Steppingmentioning

confidence: 99%

“…The corresponding network of motor cycles provides a unified description for all motor properties that have been determined by single molecule experiments. For kinesin, the experimentally observed properties include motor velocity [9,16,17], bound state diffusion coefficient (or randomness parameter) [16], ratio of forward to backward steps [9], dwell time distributions [9], and run length [18] as functions of ATP concentration and load force as well as motor velocity as a function of P and ADP concentration [19].…”

Section: Introductionmentioning

confidence: 99%

Energy Conversion by Molecular Motors Coupled to Nucleotide Hydrolysis

2009

View full text Add to dashboard Cite

Recent theoretical work on the energy conversion by molecular motors coupled to nucleotide hydrolysis is reviewed. The most abundant nucleotide is provided by adenosine triphosphate (ATP) which is cleaved into adenosine diphosphate (ADP) and inorganic phosphate. The motors have several catalytic domains (or active sites), each of which can be empty or occupied by ATP or ADP. The chemical composition of all catalytic domains defines distinct nucleotide states of the motor which form a discrete state space. Each of these motor states is connected to several other states via chemical transitions. For stepping motors such as kinesin, which walk along cytoskeletal filaments, some motor states are also connected by mechanical transitions, during which the motor is displaced along the filament and able to perform mechanical work. The different motor states together with the possible chemical and mechanical transitions provide a network representation for the chemomechanical coupling of the motor molecule. The stochastic motor dynamics on these networks exhibits several distinct motor cycles, which represent the dominant pathways for different regimes of nucleotide concentrations and load force. For the kinesin motor, the competition of two such cycles determines the stall force, at which the motor velocity vanishes and the motor reverses its direction of motion. In general, kinesin is found to be governed by the competition of three distinct chemomechanical cycles. The corresponding network representation provides a unified description for all motor properties that have been determined by single molecule experiments.

show abstract

Chemomechanical coupling of the forward and backward steps of single kinesin molecules

Cited by 288 publications

References 41 publications

Enhanced Diffusion of Molecular Motors in the Presence of Adenosine Triphosphate and External Force

Enhanced Diffusion of Molecular Motors in the Presence of Adenosine Triphosphate and External Force

Walking motion of an overdamped active particle in a ratchet potential

Energy Conversion by Molecular Motors Coupled to Nucleotide Hydrolysis

Contact Info

Product

Resources

About