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Molecular Characterization of a Cytoplasmic Dynein from Dictyostelium (1994)

KOONCE, MICHAEL P. ; GRISSOM, PAULA M. ; LYON, MARY ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

The @journal of eukaryotic microbiology 41 (1994), S. 0

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ISSN: 1550-7408

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Cytoplasmic dynein is a high molecular weight, microtubule-based mechanochemical ATPase that is believed to provide motive force for a number of intracellular motilities, including transport of membrane-bound organelles. Cytoplasmic dynein also localizes to the mitotic spindles of some organisms and to the kinetochore regions of some condensed chromosomes, where it may play an active role in spindle assembly, spindle position, and/or chromosome movement during cell division. Despite active research efforts from a number of laboratories, little detail is yet available about dynein-based cellular activities. This paper describes our efforts to characterize cytoplasmic dynein from Dictyostelium and to use this protist as a molecular genetic factory to probe structure-function relationships of this molecule.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1550-7408.1994.tb01528.x

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Two distinct isoforms of sea urchin egg dynein (1992)

Grissom, Paula M. ; Porter, Mary E. ; McIntosh, J. Richard

New York, NY : Wiley-Blackwell

Cell Motility and the Cytoskeleton 21 (1992), S. 281-292

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ISSN: 0886-1544

Keywords: ATPase ; CTPase ; minus-end-directed microtubule motility ; cytoplasmic dynein ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: Extracts of unfertilized sea urchin eggs contain at least two isoforms of cytoplasmic dynein. One exhibits a weak affinity for microtubules and is primarily soluble. The other isoform, HMr-3, binds to microtubules in an ATP-sensitive manner, but is immunologically distinct from the soluble egg dynein (Porter et al.: Journal of Biological Chemistry 263:6759-6771, 1988). We have now further distinguished these egg dynein isoforms based on differences in NTPase activity. HMr-3 copurifies with NTPase activity, but it hydrolyzes CTP at 10 times the rate of ATP. The soluble egg dynein is similar to flagellar dynein in its nucleotide specificity; its MgCTPase activity is ca. 60% of its MgATPase activity. Non-ionic detergents and salt activate the MgATPase activities of both enzymes relative to their MgCTPase activities, but this effect is more pronounced for the soluble egg dynein than for HMr-3. Sucrose gradient-purified HMr-3 promotes an ATP-sensitive microtubule bundling, as seen with darkfield optics. We have also isolated a 20 S microtubule translocating activity by sucrose gradient fractionation of egg extracts, followed by microtubule affinity and ATP release. This 20 S fraction, which contains the HMr-3 isoform, induces a microtubule gliding activity that is distinct from kinesin. Our observations suggest that soluble dynein resembles axonemal dynein, but that HMr-3 is related to the dynein-like enzymes isolated from a variety of cell types and may represent the cytoplasmic dynein of sea urchin eggs.

Additional Material: 6 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/cm.970210404

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