Unknown

Dataset Information

0

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. 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.

SUBMITTER: Jenni S 

PROVIDER: S-EPMC6815591 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure of the DASH/Dam1 complex shows its role at the yeast kinetochore-microtubule interface.

Jenni Simon S   Harrison Stephen C SC  

Science (New York, N.Y.) 20180501 6388


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  ...[more]

Similar Datasets

| S-SCDT-10_15252-EMBJ_2022112600 | biostudies-other
| S-EPMC1924804 | biostudies-other
| S-EPMC7497780 | biostudies-literature
| S-EPMC1502546 | biostudies-literature
| S-EPMC3542791 | biostudies-literature
| S-EPMC2922140 | biostudies-literature
| S-EPMC4821239 | biostudies-literature
2016-03-01 | PXD003678 | Pride
| S-EPMC8159575 | biostudies-literature
| S-EPMC3216659 | biostudies-literature