The Highly Processive Kinesin-8, Kip3, Switches Microtubule Protofilaments with a Bias toward the Left

被引:50
作者
Bormuth, Volker [1 ]
Nitzsche, Bert [1 ,2 ]
Ruhnow, Felix [1 ,2 ]
Mitra, Aniruddha [1 ,2 ]
Storch, Marko [1 ]
Rammner, Burkhard [3 ]
Howard, Jonathon [1 ]
Diez, Stefan [1 ,2 ]
机构
[1] Max Planck Inst Mol Cell Biol & Genet, Dresden, Germany
[2] Tech Univ Dresden, B CUBE Ctr Mol Bioengn, D-01062 Dresden, Germany
[3] Scimotion, Hamburg, Germany
关键词
TORQUE GENERATION; COMPONENT; MOTILITY; TRACKING; PROTEIN; DOMAIN; MOTORS;
D O I
10.1016/j.bpj.2012.05.024
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Kinesin-1 motor proteins walk parallel to the protofilament axes of microtubules as they step from one tubulin dimer to the next. Is protofilament tracking an inherent property of processive kinesin motors, like kinesin-1, and what are the structural determinants underlying protofilament tracking? To address these questions, we investigated the tracking properties of the processive kinesin-8, Kip3. Using in vitro gliding motility assays, we found that Kip3 rotates microtubules counterclockwise around their longitudinal axes with periodicities of similar to 1 mu m. These rotations indicate that the motors switch protofilaments with a bias toward the left. Molecular modeling suggests 1), that the protofilament switching may be due to kinesin-8 having a longer neck linker than kinesin-1, and 2), that the leftward bias is due the asymmetric geometry of the motor neck linker complex.
引用
收藏
页码:L04 / L06
页数:3
相关论文
共 16 条
[1]   Torque Generation of Kinesin Motors Is Governed by the Stability of the Neck Domain [J].
Brunnbauer, Melanie ;
Dombi, Renate ;
Ho, Thi-Hieu ;
Schliwa, Manfred ;
Rief, Matthias ;
Oekten, Zeynep .
MOLECULAR CELL, 2012, 46 (02) :147-158
[2]   Insights into the Mechanical Properties of the Kinesin Neck Linker Domain from Sequence Analysis and Molecular Dynamics Simulations [J].
Hariharan, Venkatesh ;
Hancock, William O. .
CELLULAR AND MOLECULAR BIOENGINEERING, 2009, 2 (02) :177-189
[3]   High-resolution cryo-EM maps show the nucleotide binding pocket of KIF1A in open and closed conformations [J].
Kikkawa, Masahide ;
Hirokawa, Nobutaka .
EMBO JOURNAL, 2006, 25 (18) :4187-4194
[4]   Phe crystal structure of dimeric kinesin and implications for microtubule-dependent motility [J].
Kozielski, F ;
Sack, S ;
Marx, A ;
Thormählen, M ;
Schönbrunn, E ;
Biou, V ;
Thompson, A ;
Mandelkow, EM ;
Mandelkow, E .
CELL, 1997, 91 (07) :985-994
[5]   Quantum-dot-assisted characterization of microtubule rotations during cargo transport [J].
Nitzsche, Bert ;
Ruhnow, Felix ;
Diez, Stefan .
NATURE NANOTECHNOLOGY, 2008, 3 (09) :552-556
[6]   Torque generation by one of the motor subunits of heterotrimeric kinesin-2 [J].
Pan, Xiaoyu ;
Acar, Seyda ;
Scholey, Jonathan M. .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2010, 401 (01) :53-57
[7]   KINESIN FOLLOWS THE MICROTUBULES PROTOFILAMENT AXIS [J].
RAY, S ;
MEYHOFER, E ;
MILLIGAN, RA ;
HOWARD, J .
JOURNAL OF CELL BIOLOGY, 1993, 121 (05) :1083-1093
[8]   A structural change in the kinesin motor protein that drives motility [J].
Rice, S ;
Lin, AW ;
Safer, D ;
Hart, CL ;
Naber, N ;
Carragher, BO ;
Cain, SM ;
Pechatnikova, E ;
Wilson-Kubalek, EM ;
Whittaker, M ;
Pate, E ;
Cooke, R ;
Taylor, EW ;
Milligan, RA ;
Vale, RD .
NATURE, 1999, 402 (6763) :778-784
[9]   Tracking Single Particles and Elongated Filaments with Nanometer Precision [J].
Ruhnow, Felix ;
Zwicker, David ;
Diez, Stefan .
BIOPHYSICAL JOURNAL, 2011, 100 (11) :2820-2828
[10]   Neck Linker Length Determines the Degree of Processivity in Kinesin-1 and Kinesin-2 Motors [J].
Shastry, Shankar ;
Hancock, William O. .
CURRENT BIOLOGY, 2010, 20 (10) :939-943