Slow ADP‐dependent acceleration of microtubule translocation produced by an axonemal dynein

FEBS Letters

Kikushima, Kenji¹  Yagi, Toshiki¹  Kamiya, Ritsu¹ 

[1] Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

关键词: Flagellum;    Inner-arm dynein;    In vitro motility assay;    ADP;    Chlamydomonas;   

DOI  :  10.1016/S0014-5793(04)00278-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Dynein has four nucleotide binding sites, of which the functional significance is unknown except for the single catalytic site. To obtain clues to the function of non-catalytic nucleotide binding, we examined the effect of ADP on the in vitro motility of Chlamydomonas inner-arm dynein species ‘a’. Upon continuous perfusion with ATP and ADP, microtubules glided on a dynein-coated glass surface with a velocity that gradually increased over a few minutes. The velocity increased faster at higher ADP concentrations. These results suggest that this dynein is activated by nucleotide binding to regulatory site(s) through an extremely slow process.

【 授权许可】

Unknown