4it3 | pdb_00004it3
Crystal Structure of Iml3 from S. cerevisiae
Structural highlights
FunctionCENPL_YEAST Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.[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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