Myosin VI Walks "Wiggly" on Actin with Large and Variable Tilting Export

@article{citeulike:2244574, abstract = {Summary Myosin VI is an unconventional motor protein with unusual motility properties such as its direction of motion and path on actin and a large stride relative to its short lever arms. To understand these features, the rotational dynamics of the lever arm were studied by single-molecule polarized total internal reflection fluorescence (polTIRF) microscopy during processive motility of myosin VI along actin. The axial angle is distributed in two peaks, consistent with the hand-over-hand model. The changes in lever arm angles during discrete steps suggest that it exhibits large and variable tilting in the plane of actin and to the sides. These motions imply that, in addition to the previously suggested flexible tail domain, there is a compliant region between the motor domain and lever arm that allows myosin VI to accommodate the helical position of binding sites while taking variable step sizes along the actin filament.}, author = {Sun, Yujie and Schroeder and Beausang, John F. and Homma, Kazuaki and Ikebe, Mitsuo and Goldman, Yale E.}, citeulike-article-id = {2244574}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.molcel.2007.10.029}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18158894}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18158894}, citeulike-linkout-3 = {http://www.sciencedirect.com/science/article/B6WSR-4RFK5HH-4/2/030207c71d8c5948b047a5f1389b1bf5}, day = {28}, doi = {10.1016/j.molcel.2007.10.029}, journal = {Molecular Cell}, keywords = {angle, fixed-dipole, fluorophore-angle, myosin, myosin-vi, poltirf, single-molecule}, month = {December}, number = {6}, pages = {954--964}, posted-at = {2008-02-29 19:52:36}, priority = {0}, title = {Myosin VI Walks "Wiggly" on Actin with Large and Variable Tilting}, url = {http://dx.doi.org/10.1016/j.molcel.2007.10.029}, volume = {28}, year = {2007} }

TY - JOUR ID - citeulike:2244574 L3 - citeulike-article-id:2244574 N2 - Summary Myosin VI is an unconventional motor protein with unusual motility properties such as its direction of motion and path on actin and a large stride relative to its short lever arms. To understand these features, the rotational dynamics of the lever arm were studied by single-molecule polarized total internal reflection fluorescence (polTIRF) microscopy during processive motility of myosin VI along actin. The axial angle is distributed in two peaks, consistent with the hand-over-hand model. The changes in lever arm angles during discrete steps suggest that it exhibits large and variable tilting in the plane of actin and to the sides. These motions imply that, in addition to the previously suggested flexible tail domain, there is a compliant region between the motor domain and lever arm that allows myosin VI to accommodate the helical position of binding sites while taking variable step sizes along the actin filament. IS - 6 JF - Molecular Cell EP - 964 TI - Myosin VI Walks "Wiggly" on Actin with Large and Variable Tilting VL - 28 SP - 954 KW - angle KW - fixed-dipole KW - fluorophore-angle KW - myosin KW - myosin-vi KW - poltirf KW - single-molecule AU - Sun, Yujie AU - Schroeder AU - Beausang, John AU - Homma, Kazuaki AU - Ikebe, Mitsuo AU - Goldman, Yale PY - 2007/12/28/ UR - http://dx.doi.org/10.1016/j.molcel.2007.10.029 ER -