Molecular Biology of the Cell click for CBE Life Science Education Page

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print April 25, 2007
Mol. Biol. Cell 10.1091/mbc.E07-02-0135

A more recent version of this article appeared on July 1, 2007
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E07-02-0135v1
18/7/2503    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Miranda, J. J.L.
Right arrow Articles by Harrison, S. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Miranda, J. J.L.
Right arrow Articles by Harrison, S. C.

Submitted on February 16, 2007
Revised on April 10, 2007
Accepted on April 17, 2007

Protein Arms in the Kinetochore-Microtubule Interface of the Yeast DASH Complex

J. J.L. Miranda,*{dagger} David S. King,{ddagger} and Stephen C. Harrison{sect}

*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138; {ddagger}Department of Molecular and Cell Biology, and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720; {sect}Department of Biological Chemistry and Molecular Pharmacology, and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115

Monitoring Editor: Kerry Bloom

The yeast DASH complex is a heterodecameric component of the kinetochore necessary for accurate chromosome segregation. DASH forms closed rings around microtubules with a large gap between the DASH ring and the microtubule cylinder. We characterized the microtubule binding properties of limited proteolysis products and subcomplexes of DASH, thus identifying candidate polypeptide extensions involved in establishing the DASH-microtubule interface. The acidic C-terminal extensions of tubulin subunits are not essential for DASH binding. We also measured the molecular mass of DASH rings on microtubules with scanning transmission electron microscopy and found that approximately twenty-five DASH heterodecamers assemble to form each ring. Dynamic association and relocation of multiple flexible appendages of DASH may allow the kinetochore to translate along the microtubule surface.

{dagger}Present address: Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158.

Address correspondence to: Stephen C. Harrison (harrison{at}crystal.harvard.edu)




This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
E. Nogales and V. H. Ramey
Structure-function insights into the yeast Dam1 kinetochore complex
J. Cell Sci., November 1, 2009; 122(21): 3831 - 3836.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
E. L. Grishchuk, A. K. Efremov, V. A. Volkov, I. S. Spiridonov, N. Gudimchuk, S. Westermann, D. Drubin, G. Barnes, J. R. McIntosh, and F. I. Ataullakhanov
The Dam1 ring binds microtubules strongly enough to be a processive as well as energy-efficient coupler for chromosome motion
PNAS, October 7, 2008; 105(40): 15423 - 15428.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
E. L. Grishchuk, I. S. Spiridonov, V. A. Volkov, A. Efremov, S. Westermann, D. Drubin, G. Barnes, F. I. Ataullakhanov, and J. R. McIntosh
Different assemblies of the DAM1 complex follow shortening microtubules by distinct mechanisms
PNAS, May 13, 2008; 105(19): 6918 - 6923.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. Efremov, E. L. Grishchuk, J. R. McIntosh, and F. I. Ataullakhanov
In search of an optimal ring to couple microtubule depolymerization to processive chromosome motions
PNAS, November 27, 2007; 104(48): 19017 - 19022.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.