CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like fold.
Cell
; 148(3): 487-501, 2012 Feb 03.
Article
in En
| MEDLINE
| ID: mdl-22304917
ABSTRACT
The multiprotein kinetochore complex must assemble at a specific site on each chromosome to achieve accurate chromosome segregation. Defining the nature of the DNA-protein interactions that specify the position of the kinetochore and provide a scaffold for kinetochore formation remain key goals. Here, we demonstrate that the centromeric histone-fold-containing CENP-T-W and CENP-S-X complexes coassemble to form a stable CENP-T-W-S-X heterotetramer. High-resolution structural analysis of the individual complexes and the heterotetramer reveals similarity to other histone fold-containing complexes including canonical histones within a nucleosome. The CENP-T-W-S-X heterotetramer binds to and supercoils DNA. Mutants designed to compromise heterotetramerization or the DNA-protein contacts around the heterotetramer strongly reduce the DNA binding and supercoiling activities in vitro and compromise kinetochore assembly in vivo. These data suggest that the CENP-T-W-S-X complex forms a unique nucleosome-like structure to generate contacts with DNA, extending the "histone code" beyond canonical nucleosome proteins.
Full text:
1
Database:
MEDLINE
Main subject:
Chromosomal Proteins, Non-Histone
/
Centromere
/
Chickens
/
DNA-Binding Proteins
Limits:
Animals
/
Humans
Language:
En
Year:
2012
Type:
Article