期刊
CELL
卷 133, 期 3, 页码 427-439出版社
CELL PRESS
DOI: 10.1016/j.cell.2008.03.020
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资金
- NCI NIH HHS [K01 CA125051] Funding Source: Medline
- NIGMS NIH HHS [R37 GM024364] Funding Source: Medline
- Telethon [GGP06044] Funding Source: Medline
- Associazione Italiana per la Ricerca sul Cancro Funding Source: Custom
Kinetochores are proteinaceous assemblies that mediate the interaction of chromosomes with the mitotic spindle. The 180 kDa Ndc80 complex is a direct point of contact between kinetochores and microtubules. Its four subunits contain coiled coils and form an elongated rod structure with functional globular domains at either end. We crystallized an engineered bonsai'' Ndc80 complex containing a shortened rod domain but retaining the globular domains required for kinetochore localization and microtubule binding. The structure reveals a microtubule-binding interface containing a pair of tightly interacting calponin-homology (CH) domains with a previously unknown arrangement. The interaction with microtubules is cooperative and predominantly electrostatic. It involves positive charges in the CH domains and in the N-terminal tail of the Ndc80 subunit and negative charges in tubulin C-terminal tails and is regulated by the Aurora B kinase. We discuss our results with reference to current models of kinetochore-microtubule attachment and centromere organization.
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