Main Menu (Mobile)- Block

Main Menu - Block

custom | custom

Search Results

filters_region_cap | custom

Filter

facetapi-Q2b17qCsTdECvJIqZJgYMaGsr8vANl1n | block

Associated Lab

facetapi-PV5lg7xuz68EAY8eakJzrcmwtdGEnxR0 | block

Publication Date

general_search_page-panel_pane_1 | views_panes

1 Janelia Publications

Showing 1-1 of 1 results
Your Criteria:
    Wu Lab
    10/01/17 | Molecular basis of CENP-C association with the CENP-A nucleosome at yeast centromeres.
    Xiao H, Wang F, Wisniewski J, Shaytan AK, Ghirlando R, Fitzgerald PC, Huang Y, Wei D, Li S, Landsman D, Panchenko AR, Wu C
    Genes & Development. 2017 Oct 01;31(19):1958-1972. doi: 10.1101/gad.304782.117

    Histone CENP-A-containing nucleosomes play an important role in nucleating kinetochores at centromeres for chromosome segregation. However, the molecular mechanisms by which CENP-A nucleosomes engage with kinetochore proteins are not well understood. Here, we report the finding of a new function for the budding yeast Cse4/CENP-A histone-fold domain interacting with inner kinetochore protein Mif2/CENP-C. Strikingly, we also discovered that AT-rich centromere DNA has an important role for Mif2 recruitment. Mif2 contacts one side of the nucleosome dyad, engaging with both Cse4 residues and AT-rich nucleosomal DNA. Both interactions are directed by a contiguous DNA- and histone-binding domain (DHBD) harboring the conserved CENP-C motif, an AT hook, and RK clusters (clusters enriched for arginine-lysine residues). Human CENP-C has two related DHBDs that bind preferentially to DNA sequences of higher AT content. Our findings suggest that a DNA composition-based mechanism together with residues characteristic for the CENP-A histone variant contribute to the specification of centromere identity.

    View Publication Page