Porters versus rowers: a unified stochastic model of motor proteins.
We present a general phenomenological theory for chemical to mechanical energy transduction by motor enzymes which is based on the classical "tight-coupling" mechanism. The associated minimal stochastic model takes explicitly into account both ATP hydrolysis and thermal noise effects. It provides expressions for the hydrolysis rate and the sliding velocity, as functions of the ATP concentration and the number of motor enzymes. It explains in a unified way many results of recent in vitro motility assays. More importantly, the theory provides a natural classification scheme for the motors: it correlates the biochemical and mechanical differences between "porters" such as cellular kinesins or dyneins, and "rowers" such as muscular myosins or flagellar dyneins.
Department of Physics, Princeton University, New Jersey 08544.
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Leibler
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Huse
D000199:Actins / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001692:Biological Transport / Q000502:physiology; D003593:Cytoplasm; D004398:Dyneins / Q000502:physiology*; D004734:Energy Metabolism; D005407:Flagella; D017276:Friction; D016547:Kinesins / Q000502:physiology*; D007700:Kinetics; D008870:Microtubules / Q000378:metabolism; D008954:Models, Biological; D008956:Models, Chemical; D015233:Models, Statistical; D009068:Movement / Q000502:physiology; D009132:Muscles / Q000378:metabolism; D009218:Myosins / Q000502:physiology*; D011485:Protein Binding; D013269:Stochastic Processes
D000199:Actins; D000255:Adenosine Triphosphate; D009218:Myosins; D004398:Dyneins; D016547:Kinesins