4it3 | pdb_00004it3
Crystal Structure of Iml3 from S. cerevisiae
Structural highlights
Function[IML3_YEAST] Component of the central kinetochore, which mediates the attachment of the centromere to the mitotic spindle by forming essential interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. Required for establishing bipolar spindle-microtubule attachments and proper chromosome segregation.[1] [2] Publication Abstract from PubMedAccurate 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. An Iml3-Chl4 Heterodimer Links the Core Centromere to Factors Required for Accurate Chromosome Segregation.,Hinshaw SM, Harrison SC Cell Rep. 2013 Sep 25. pii: S2211-1247(13)00477-4. doi:, 10.1016/j.celrep.2013.08.036. PMID:24075991[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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