Slow ADP-dependent acceleration of microtubule translocation produced by an axonemal dynein.
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.
Kikushima
Kenji
K
Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Yagi
Toshiki
T
Kamiya
Ritsu
R
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
D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D004398:Dyneins