Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans.
C. elegans contains a microtubule binding protein that resembles both dynein and kinesin. This protein has a MgATPase activity and copurifies on both sucrose gradients and DEAE Sephadex columns with a polypeptide of Mr approximately 400 kd. The ATPase activity is 50% inhibited by 10 microM vanadate, 1 mM N-ethyl maleimide, or 5 mM AMP-PNP; it is enhanced 50% by 0.2% Triton. The 400 kd polypeptide is cleaved at a single site by ultraviolet light in the presence of ATP and vanadate. In these ways, the protein resembles dynein. The protein also promotes ATP-dependent translocation of microtubules or axonemes, "plus" ends trailing. This property is kinesin-like; however, the motility is blocked by 5 microM vanadate, 1 mM N-ethyl maleimide, 0.5 mM ATP-gamma-S, or by ATP-vanadate-UV cleavage of the 400 kd polypeptide, characteristics that differ from kinesin. We propose that this protein is a novel microtubule translocator.
D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D002107:Caenorhabditis / Q000502:physiology*; D002465:Cell Movement / Q000187:drug effects; D003429:Cross Reactions; D003593:Cytoplasm / Q000502:physiology*; D004625:Embryo, Nonmammalian / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000032:analysis / Q000502:physiology; D008870:Microtubules / Q000502:physiology*; D008970:Molecular Weight; D017830:Octoxynol; D010455:Peptides / Q000032:analysis; D011092:Polyethylene Glycols / Q000494:pharmacology; D014466:Ultraviolet Rays
D008869:Microtubule-Associated Proteins; D010455:Peptides; D011092:Polyethylene Glycols; D017830:Octoxynol; D000251:Adenosine Triphosphatases