Journal
SCIENCE
Volume 360, Issue 6388, Pages 552-557Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aar6436
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Funding
- NIH [P41 GM103403]
- NIH-ORIP HEI grant [S10 RR029205]
- DOE Office of Science [DE-AC02-06CH11357]
- Howard Hughes Medical Institute (HHMI) Fellow of the Damon Runyon Cancer Research Foundation [DRG-2004-09]
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Kinetochores connect mitotic-spindle microtubules with chromosomes, allowing microtubule depolymerization to pull chromosomes apart during anaphase while resisting detachment as the microtubule shortens. The heterodecameric DASH/Dam1 complex (DASH/Dam1c), an essential component of yeast kinetochores, assembles into a microtubule-encircling ring. The ring associates with rodlike Ndc80 complexes to organize the kinetochore-microtubule interface. We report the cryo-electron microscopy structure (at similar to 4.5-angstrom resolution) of a DASH/Dam1c ring and a molecular model of its ordered components, validated by evolutionary direct-coupling analysis. Integrating this structure with that of the Ndc80 complex and with published interaction data yields a molecular picture of kinetochore-microtubule attachment, including how flexible, C-terminal extensions of DASH/Dam1c subunits project and contact widely separated sites on the Ndc80 complex rod and how phosphorylation at previously identified sites might regulate kinetochore assembly.
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