title: Slow ADP-dependent acceleration of microtubule translocation produced by an axonemal dynein.
abstract: 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.
authors.affiliation: Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Kikushima
authors.forename: Toshiki
authors.initials: T
authors.lastname: Yagi
authors.forename: Ritsu
authors.initials: R
authors.lastname: Kamiya
mesh_terms: D000054:Acceleration; D000244:Adenosine Diphosphate / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001369:Axons / Q000737:chemistry*; D001483:Base Sequence; D001665:Binding Sites; D001681:Biological Assay; D002696:Chlamydomonas / Q000201:enzymology / Q000378:metabolism; D004398:Dyneins / Q000737:chemistry / Q000378:metabolism*; D005407:Flagella / Q000201:enzymology / Q000378:metabolism; D007700:Kinetics; D008870:Microtubules / Q000201:enzymology* / Q000378:metabolism / Q000502:physiology; D009068:Movement
chemical_list: D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D004398:Dyneins