Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface
Abstract
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. Here, we report the cryo–electron microscopy structure (at ~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.
- Authors:
-
[1];
[2]
- Harvard Medical School, Boston, MA (United States)
- Harvard Medical School, Boston, MA (United States); Howard Hughes Medical Inst., Chevy Chase, MD (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE Office of Science (SC); National Institutes of Health (NIH); Damon Runyon Cancer Research Foundation
- OSTI Identifier:
- 1438840
- Grant/Contract Number:
- AC02-06CH11357; P41 GM103403; S10 RR029205; DRG-2004-09
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Science
- Additional Journal Information:
- Journal Volume: 360; Journal Issue: 6388; Journal ID: ISSN 0036-8075
- Publisher:
- AAAS
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Jenni, Simon, and Harrison, Stephen C. Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface. United States: N. p., 2018.
Web. doi:10.1126/science.aar6436.
Jenni, Simon, & Harrison, Stephen C. Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface. United States. https://doi.org/10.1126/science.aar6436
Jenni, Simon, and Harrison, Stephen C. Fri .
"Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface". United States. https://doi.org/10.1126/science.aar6436. https://www.osti.gov/servlets/purl/1438840.
@article{osti_1438840,
title = {Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface},
author = {Jenni, Simon and Harrison, Stephen C.},
abstractNote = {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. Here, we report the cryo–electron microscopy structure (at ~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.},
doi = {10.1126/science.aar6436},
journal = {Science},
number = 6388,
volume = 360,
place = {United States},
year = {Fri May 04 00:00:00 EDT 2018},
month = {Fri May 04 00:00:00 EDT 2018}
}
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