Different assemblies of the DAM1 complex follow shortening microtubules by distinct mechanisms

Mitotic chromosomes segregate at the ends of shortening spindle microtubules (MTs). In budding yeast, the Dam1 multiprotein complex supports this dynamic attachment, thereby contributing to accurate chromosome segregation. Purified Dam1 will track the end of a depolymerizing MT and can couple it to...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2008-05, Vol.105 (19), p.6918-6923
Main Authors: Grishchuk, E.L, Spiridonov, I.S, Volkov, V.A, Efremov, A, Westermann, S, Drubin, D, Barnes, G, Ataullakhanov, F.I, McIntosh, J.R
Format: Article
Language:English
Subjects:
Animals
Biological Sciences
Biological Transport
Cell Cycle Proteins - metabolism
Cell division
Cell Polarity
Cells
Chlamydomonas
Chromosomes
Dams
Depolymerization
Diffusion
Fluorescence
Kinetics
Kinetochores
Microspheres
Microtubule-Associated Proteins - metabolism
Microtubules
Microtubules - metabolism
Molecular Weight
Oligomers
Protein Structure, Quaternary
Protein Subunits - metabolism
Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Saccharomycetales
Solubility
Solutions
Tetrahymena
Yeast
Yeasts
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Summary:Mitotic chromosomes segregate at the ends of shortening spindle microtubules (MTs). In budding yeast, the Dam1 multiprotein complex supports this dynamic attachment, thereby contributing to accurate chromosome segregation. Purified Dam1 will track the end of a depolymerizing MT and can couple it to microbead transport in vitro. The processivity of such motions has been thought to depend on rings that the Dam1 complex can form around MTs, but the possibility that alternative coupling geometries contribute to these motilities has not been considered. Here, we demonstrate that both rings and nonencircling Dam1 oligomers can track MT ends and enable processive cargo movement in vitro. The coupling properties of these two assemblies are, however, quite different, so each may make a distinct contribution to chromosome motility.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0801811105