Abstract
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.
MeSH Terms
Animals
Biological Transport
Cell Cycle Proteins/metabolism
Cell Polarity
Chlamydomonas
Diffusion
Microspheres
Microtubule-Associated Proteins/metabolism
Microtubules/metabolism
Molecular Weight
Protein Structure, Quaternary
Protein Subunits/metabolism
Saccharomyces cerevisiae/cytology,metabolism
Saccharomyces cerevisiae Proteins/metabolism
Solubility
Solutions
Tetrahymena
Chemicals
Cell Cycle Proteins
DAM1 protein, S cerevisiae
Microtubule-Associated Proteins
Protein Subunits
Saccharomyces cerevisiae Proteins
Solutions
Authors & Affiliations
9 authors, click to expand affiliations / ORCID
Grishchuk E L
Molecular, Cellular, and Developmental Biology Department, University of Colorado, Boulder, CO 80309, USA.
Spiridonov I S
Volkov V A
Efremov A
Westermann S
Drubin D
Barnes G
Ataullakhanov F I
McIntosh J R
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