Publications [#113159] of Harold P. Erickson
- MD Neely, HP Erickson, K Boekelheide, HMW-2, the Sertoli cell cytoplasmic dynein from rat testis, is a dimer composed of nearly identical subunits.,
The Journal of biological chemistry, UNITED STATES, vol. 265 no. 15
pp. 8691-8, ISSN 0021-9258
(last updated on 2009/02/12)
The ultrastructure and biochemical characteristics of HMW-2, the Sertoli cell cytoplasmic dynein isolated from rat testes, were analyzed. Electron microscopic studies revealed a two-headed two-stem structure with dimensions very similar to other dyneins. We found that, like other cytoplasmic dyneins, both heads have an approximately spherical shape with a central cavity. Heavy chain analysis suggested the presence of only one type of heavy chain, a finding that was supported by the simple Michaelis-Menten kinetics displayed by the HMW-2-associated ATPase activity. In addition, dissociation of the HMW-2 complex resulted in a single type of dynein subunit sedimenting at 11.8 S. This fraction contained all the polypeptides present in the undissociated HMW-2. Ultrastructurally the HMW-2 subunits were composed of one globular domain with a tail. The simplest interpretation is that HMW-2 is a dimer of nearly identical subunits, each containing one heavy chain, one 90-kDa intermediate chain, and two light chains.
Adenosine Triphosphatases • Animals • Cytoplasm • Dynein ATPase • Macromolecular Substances • Male • Microscopy, Electron • Molecular Weight • Rats • Sertoli Cells • enzymology • enzymology* • isolation & purification* • ultrastructure