Fitzpatrick Institute for Photonics Fitzpatrick Institute for Photonics
Pratt School of Engineering
Duke University

 HOME > pratt > FIP    Search Help Login pdf version printable version 

Publications [#64081] of Harold P. Erickson

Papers Published

  1. Chandra, Rashmi and Salmon, Edward D. and Erickson, Harold P. and Lockhart, Andrew and Endow, Sharyn A., Structural and functional domains of the Drosophila ncd microtubule motor protein, Journal of Biological Chemistry, vol. 268 no. 12 (1993), pp. 9005 - 9013
    (last updated on 2007/04/15)

    Abstract:
    Nonclaret disjunctional (ncd) is a kinesin-related microtubule motor protein that is required for proper chromosome distribution in Drosophila. Despite its sequence similarity to kinesin heavy chain, ncd translocates with the opposite polarity as kinesin, toward microtubule minus ends. We have expressed different regions of the protein in bacteria and analyzed the proteins for function. Results indicate that ncd consists of three domains: a basic, proline-rich N-terminal "tail," a central α-helical coiled-coil stalk, and a C-terminal motor domain. The ncd N terminus proteins bundle microtubules in motility assays and show ATP-independent binding to microtubules in solution. Truncated proteins, lacking the tail but containing the predicted motor domain and differing lengths of the stalk, did not support microtubule gliding in in vitro assays but showed microtubule-stimulated MgATPase activity in solution. Addition of a nonspecific N terminus to two of the truncated proteins restored directional gliding and rotation of microtubules in motility assays, demonstrating that these properties map to the predicted mechanochemical domain of ncd. Physical properties of the C terminus proteins indicate that the stalk region is important for dimerization and that the ncd protein probably exists and functions as a dimer.


Duke University * Pratt * Reload * Login