TY - JOUR
T1 - Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3
AU - Arimura, Yasuhiro
AU - Shirayama, Kazuyoshi
AU - Horikoshi, Naoki
AU - Fujita, Risa
AU - Taguchi, Hiroyuki
AU - Kagawa, Wataru
AU - Fukagawa, Tatsuo
AU - Almouzni, Geneviève
AU - Kurumizaka, Hitoshi
PY - 2014
Y1 - 2014
N2 - The centromere-specific histone H3 variant, CENP-A, is overexpressed in particular aggressive cancer cells, where it can be mislocalized ectopically in the form of heterotypic nucleosomes containing H3.3. In the present study, we report the crystal structure of the heterotypic CENP-A/H3.3 particle and reveal its "hybrid structure", in which the physical characteristics of CENP-A and H3.3 are conserved independently within the same particle. The CENP-A/H3.3 nucleosome forms an unexpectedly stable structure as compared to the CENP-A nucleosome, and allows the binding of the essential centromeric protein, CENP-C, which is ectopically mislocalized in the chromosomes of CENP-A overexpressing cells.
AB - The centromere-specific histone H3 variant, CENP-A, is overexpressed in particular aggressive cancer cells, where it can be mislocalized ectopically in the form of heterotypic nucleosomes containing H3.3. In the present study, we report the crystal structure of the heterotypic CENP-A/H3.3 particle and reveal its "hybrid structure", in which the physical characteristics of CENP-A and H3.3 are conserved independently within the same particle. The CENP-A/H3.3 nucleosome forms an unexpectedly stable structure as compared to the CENP-A nucleosome, and allows the binding of the essential centromeric protein, CENP-C, which is ectopically mislocalized in the chromosomes of CENP-A overexpressing cells.
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U2 - 10.1038/srep07115
DO - 10.1038/srep07115
M3 - Article
C2 - 25408271
AN - SCOPUS:84927912974
SN - 2045-2322
VL - 4
SP - 7115
JO - Scientific Reports
JF - Scientific Reports
ER -