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TitleStructure of the inner kinetochore CCAN complex assembled onto a centromeric nucleosome.
Journal, issue, pagesNature, Vol. 574, Issue 7777, Page 278-282, Year 2019
Publish dateOct 2, 2019
AuthorsKaige Yan / Jing Yang / Ziguo Zhang / Stephen H McLaughlin / Leifu Chang / Domenico Fasci / Ann E Ehrenhofer-Murray / Albert J R Heck / David Barford /
PubMed AbstractIn eukaryotes, accurate chromosome segregation in mitosis and meiosis maintains genome stability and prevents aneuploidy. Kinetochores are large protein complexes that, by assembling onto specialized ...In eukaryotes, accurate chromosome segregation in mitosis and meiosis maintains genome stability and prevents aneuploidy. Kinetochores are large protein complexes that, by assembling onto specialized Cenp-A nucleosomes, function to connect centromeric chromatin to microtubules of the mitotic spindle. Whereas the centromeres of vertebrate chromosomes comprise millions of DNA base pairs and attach to multiple microtubules, the simple point centromeres of budding yeast are connected to individual microtubules. All 16 budding yeast chromosomes assemble complete kinetochores using a single Cenp-A nucleosome (Cenp-A), each of which is perfectly centred on its cognate centromere. The inner and outer kinetochore modules are responsible for interacting with centromeric chromatin and microtubules, respectively. Here we describe the cryo-electron microscopy structure of the Saccharomyces cerevisiae inner kinetochore module, the constitutive centromere associated network (CCAN) complex, assembled onto a Cenp-A nucleosome (CCAN-Cenp-A). The structure explains the interdependency of the constituent subcomplexes of CCAN and shows how the Y-shaped opening of CCAN accommodates Cenp-A to enable specific CCAN subunits to contact the nucleosomal DNA and histone subunits. Interactions with the unwrapped DNA duplex at the two termini of Cenp-A are mediated predominantly by a DNA-binding groove in the Cenp-L-Cenp-N subcomplex. Disruption of these interactions impairs assembly of CCAN onto Cenp-A. Our data indicate a mechanism of Cenp-A nucleosome recognition by CCAN and how CCAN acts as a platform for assembly of the outer kinetochore to link centromeres to the mitotic spindle for chromosome segregation.
External linksNature / PubMed:31578520 / PubMed Central
MethodsEM (single particle)
Resolution3.45 - 4.15 Å
Structure data

4579

6qld

EMDB-4579, PDB-6qld:
Structure of inner kinetochore CCAN-Cenp-A complex
Method: EM (single particle) / Resolution: 4.15 Å

4580

6qle

EMDB-4580, PDB-6qle:
Structure of inner kinetochore CCAN complex
Method: EM (single particle) / Resolution: 3.55 Å

4581

6qlf

EMDB-4581, PDB-6qlf:
Structure of inner kinetochore CCAN complex with mask1
Method: EM (single particle) / Resolution: 3.45 Å

EMDB-4971:
Structure of inner kinetochore CCAN complex
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • Saccharomyces cerevisiae (strain ATCC 204508 / S288c) cerevisiae (yeast)
  • escherichia coli (E. coli)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsDNA BINDING PROTEIN / inner kinetochore / DNA / nucleosome / CCAN / complex

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