CENP-C recruits M18BP1 to centromeres to promote CENP-A chromatin assembly

Eukaryotic chromosomes segregate by attaching to microtubules of the mitotic spindle through a chromosomal microtubule binding site called the kinetochore. Kinetochores assemble on a specialized chromosomal locus termed the centromere, which is characterized by the replacement of histone H3 in centr...

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Bibliographic Details
Published in:The Journal of cell biology 2011-09, Vol.194 (6), p.855-871
Main Authors: Moree, Ben, Meyer, Corey B, Fuller, Colin J, Straight, Aaron F
Format: Article
Language:English
Subjects:
Animals
Autoantigens - genetics
Autoantigens - metabolism
Binding Sites
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell division
CENP-C protein
Centromere - metabolism
Centromere Protein A
Chromatin
Chromatin - metabolism
Chromatin Assembly and Disassembly
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - metabolism
Chromosomes
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Eukaryotes
Fluorescent Antibody Technique
Nucleosomes - metabolism
Proteins
Xenopus Proteins - genetics
Xenopus Proteins - metabolism
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Summary:Eukaryotic chromosomes segregate by attaching to microtubules of the mitotic spindle through a chromosomal microtubule binding site called the kinetochore. Kinetochores assemble on a specialized chromosomal locus termed the centromere, which is characterized by the replacement of histone H3 in centromeric nucleosomes with the essential histone H3 variant CENP-A (centromere protein A). Understanding how CENP-A chromatin is assembled and maintained is central to understanding chromosome segregation mechanisms. CENP-A nucleosome assembly requires the Mis18 complex and the CENP-A chaperone HJURP. These factors localize to centromeres in telophase/G1, when new CENP-A chromatin is assembled. The mechanisms that control their targeting are unknown. In this paper, we identify a mechanism for recruiting the Mis18 complex protein M18BP1 to centromeres. We show that depletion of CENP-C prevents M18BP1 targeting to metaphase centromeres and inhibits CENP-A chromatin assembly. We find that M18BP1 directly binds CENP-C through conserved domains in the CENP-C protein. Thus, CENP-C provides a link between existing CENP-A chromatin and the proteins required for new CENP-A nucleosome assembly.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.201106079