Kinetochore attachments require an interaction between unstructured tails on microtubules and Ndc80(Hec1).

ABSTRACT: Kinetochore attachments to microtubules are tight enough to move chromosomes, yet the microtubules' plus ends must remain dynamic and reposition within the attachment pocket during depolymerization-coupled movement. Kinetochores are unable to bind microtubules after any of the four subunits of the Ndc80 complex are knocked down [2, 4]; however, because the Ndc80 complex has important structural roles [1-3], it is unclear whether it directly mediates kinetochore-microtubule attachments. The Ndc80(Hec1) subunit (Hec1) has a microtubule-binding site composed of both an unstructured N-terminal tail and a calponin homology domain [5-7]. Here, we show that, surprisingly, the N-terminal tail is sufficient for microtubule-binding affinity in vitro. The interaction is salt sensitive, and the positi

SUBMITTER: Miller SA 

PROVIDER: S-EPMC3145211 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature