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• W2184668114 abstract "The kinesin superfamily consists of mechanoenzymes that convert chemical energy, stored in nucleoside triphosphates, into movement along microtubules. The founding member of this protein superfamily, the so-called conventional kinesin, was only known from animal sources until the recent description of kinesin from the filamentous fungus Neurospora crassa (G.Steinberg, M.Schliwa, Mol. Biol. Cell 6, 1605-1618 (1995)). To determine whether similar motors with comparable features are common in other filamentous fungi, a kinesin from a zygomycete, Syncephalastrum racemosum, was purified. Here, the isolation and characterization of this motorenzyme is described. The purified protein consisted of a doublet at 112 kDa and 115 kDa with no addilional polypeptides. This was consistent with a calculated molecufar mass of -?,40 kDa and suggests that the motor is a dimer with a more globular shape than conventional kinesin from animal sources. In gliding assays the enzyme moved microtubules at 2,5 to 3.4 pm/s and had a nucleolide specificity similar to the Neurospora kinesin motor. Peptide antibodies against conserved regions in the head and the tail domain of conventional kinesins cross-reacted with the Syncephalastrum motor. In vitro, the enzyme was able to drive the microtubule-dependent movement of vesicles isolated from Syncephalastrum racemosum, as well as Neurospora crassa, and Aspergillus nidulans. In summary the Syncephalastrum motor has many of the unique features in common with the conventional kinesin from the ascomycete Neurospora crassa and probably shares a similar function in living hyphae." @default.
• W2184668114 created "2016-06-24" @default.
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• W2184668114 date "1997-01-01" @default.
• W2184668114 modified "2023-09-27" @default.
• W2184668114 title "A kinesin-like mechqnoenzyme from the zygomycete Syncephqlqstrum rqcemosum shores biochemicql similqrities with convenlionql kinesin from Neurosporq crqssq" @default.
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• W2184668114 hasPublicationYear "1997" @default.
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