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 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.
Grishchuk
E L
EL
Molecular, Cellular, and Developmental Biology Department, University of Colorado, Boulder, CO 80309, USA.
Spiridonov
I S
IS
Volkov
V A
VA
Efremov
A
A
Westermann
S
S
Drubin
D
D
Barnes
G
G
Ataullakhanov
F I
FI
McIntosh
J R
JR
D000818:Animals; D001692:Biological Transport; D018797:Cell Cycle Proteins / Q000378:metabolism*; D016764:Cell Polarity; D002696:Chlamydomonas; D004058:Diffusion; D008863:Microspheres; D008869:Microtubule-Associated Proteins / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D008970:Molecular Weight; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D012995:Solubility; D012996:Solutions; D013768:Tetrahymena
D018797:Cell Cycle Proteins; C116003:DAM1 protein, S cerevisiae; D008869:Microtubule-Associated Proteins; D021122:Protein Subunits; D029701:Saccharomyces cerevisiae Proteins; D012996:Solutions