![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
|
|
|
|
|
||
A more recent version of this article appeared on November 1, 2005
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on June 29, 2005
Revised on August 12, 2005
Accepted on August 25, 2005
*Stowers Institute for Medical Research, Kansas City, MO 64110; Department of Pathology and Clinical Laboratory, University of Kansas Medical Center, Kansas City, KS 66160; Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260; ||Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235; ¶Department of Molecular Biosciences, University of Kansas, Lawrence, KS 66045
Monitoring Editor: J. Richard McIntosh
Nod, a nonmotile kinesin-like protein, plays a critical role in segregating achiasmate chromosomes during female meiosis. In addition to localizing to oocyte chromosomes, we show that functional full-length Nod-GFP (NodFL-GFP) localizes to the posterior pole of the oocyte at stages 9-10A, as does Kinesin Heavy Chain (KHC), a plus end directed motor. This posterior localization is abolished in grk mutants that no longer maintain the microtubule (MT) gradient in the oocyte. To test the hypothesis that Nod binds to the plus ends of MTs, we expressed and purified both full-length Nod (NodFL) and a truncated form of Nod containing only the motor-like domain (Nod318) from E. coli, and assessed their interactions with MTs in vitro. Both NodFL and Nod318 demonstrate preferential binding to the ends of the MTs, displaying a strong preference for binding to the plus ends. When Nod318-GFP:MT collision complexes were trapped by glutaraldehyde fixation, the preference for binding to plus ends versus minus ends was 17:1. NodFL and Nod318 also promote MT polymerization in vitro in a time-dependent manner. The observation that Nod is preferentially localized to the plus ends of MTs and stimulates MT polymerization suggests a mechanism for its function.
These authors contributed equally to this work.
Address correspondence to:
R. S. Hawley (rsh{at}stowers-institute.org)
This article has been cited by other articles:
|
|
 |
|
  Y. Xiang and R. S. Hawley The Mechanism of Secondary Nondisjunction in Drosophila melanogaster Females Genetics, September 1, 2006; 174(1): 67 - 78. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. S. Shapiro and K. V. Anderson Drosophila Ik2, a member of the I{kappa}B kinase family, is required for mRNA localization during oogenesis Development, April 15, 2006; 133(8): 1467 - 1475. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W. Cui and R. S. Hawley The HhH(2)/NDD Domain of the Drosophila Nod Chromokinesin-like Protein Is Required for Binding to Chromosomes in the Oocyte Nucleus Genetics, December 1, 2005; 171(4): 1823 - 1835. [Abstract] [Full Text] [PDF]
|
|
