Premium
Nucleotide‐dependent behavior of single molecules of cytoplasmic dynein on microtubules in vitro
Author(s) -
Miura Michi,
Matsubara Aiko,
Kobayashi Takuya,
Edamatsu Masaki,
Toyoshima Yoko Y.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.04.016
Subject(s) - dynein , dynactin , microtubule , microbiology and biotechnology , nucleotide , biology , cytoplasm , biophysics , chemistry , biochemistry , gene
We visualized the nucleotide‐dependent behavior of single molecules of mammalian native cytoplasmic dynein using fragments of dynactin p150 with or without its N‐terminal microtubule binding domain. The results indicate that the binding affinity of dynein for microtubules is high in AMP‐PNP, middle in ADP or no nucleotide, and low in ADP·Pi conditions. It is also demonstrated that the microtubule binding domain of dynactin p150 maintains the association of dynein with microtubules without altering the motile property of dynein in the weak binding state. In addition, we observed bidirectional movement of dynein in the presence of ATP as well as in ADP/Vi condition, suggesting that the bidirectional movement is driven by diffusion rather than active transport.