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PDBsum entry 4je3
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References listed in PDB file
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Key reference
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Title
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An iml3-Chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation.
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Authors
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S.M.Hinshaw,
S.C.Harrison.
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Ref.
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Cell Rep, 2013,
5,
29-36.
[DOI no: ]
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PubMed id
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Abstract
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Accurate segregation of genetic material in eukaryotes relies on the
kinetochore, a multiprotein complex that connects centromeric DNA with
microtubules. In yeast and humans, two proteins-Mif2/CENP-C and
Chl4/CNEP-N-interact with specialized centromeric nucleosomes and establish
distinct but cross-connecting axes of chromatin-microtubule linkage. Proteins
recruited by Chl4/CENP-N include a subset that regulates chromosome transmission
fidelity. We show that Chl4 and a conserved member of this subset, Iml3, both
from Saccharomyces cerevisiae, form a stable protein complex that interacts with
Mif2 and Sgo1. We have determined the structures of an Iml3 homodimer and an
Iml3-Chl4 heterodimer, which suggest a mechanism for regulating the assembly of
this functional axis of the kinetochore. We propose that at the core centromere,
the Chl4-Iml3 complex participates in recruiting factors, such as Sgo1, that
influence sister chromatid cohesion and encourage sister kinetochore
biorientation.
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