2004/11/11 by Ping Xie, Shuo-Xing Dou, Xie, Ping +5
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Chemistry · #Biology #Biomolecules (q-bio.BM) #Biophysics #Cell biology #Chemistry #Dynein #FOS: Biological sciences #Microtubule #Microtubule and mitosis dynamics #Photosynthetic Processes and Mechanisms #Physics #Plant Molecular Biology Research #Stalk #q-bio.BM
paper · pdf · doi:10.48550/arxiv.q-bio/0411023
16 pages, 5 figures
arxiv created 2004/11/11 · openalex publication_date 2004/11/11 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
A model for the processive movement of dynein is presented based on experimental observations available. In the model, the change from strong microtubule-binding to weak binding of dynein is determined naturally by the variation of the relative orientation between the two interacting surfaces of the stalk tip and the microtubule as the stalk rotates from the ADP.Vi-state orientation to the apo-state orientation. This means that the puzzling communication from the ATP binding site in the globular head to the MT-binding site in the tip of the stalk, which is prerequisite in the conventional model, is not required. Using the present model, the previous experimental results, such as (i) the step size of a dynein being an integer times of the period of the MT lattice, (ii) the dependence of the step size on load, i.e., the step size decreasing with the increase of load, and (iii) the stall force being proportional to [ATP] at low [ATP] and becoming saturated at high [ATP], are well explained.