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• W1990276386 endingPage "318" @default.
• W1990276386 startingPage "309" @default.
• W1990276386 abstract "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." @default.
• W1990276386 created "2016-06-24" @default.
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• W1990276386 date "1987-10-01" @default.
• W1990276386 modified "2023-10-16" @default.
• W1990276386 title "Identification of a microtubule-based cytoplasmic motor in the nematode C. elegans" @default.
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• W1990276386 doi "https://doi.org/10.1016/0092-8674(87)90157-7" @default.
• W1990276386 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2959372" @default.
• W1990276386 hasPublicationYear "1987" @default.
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