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Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3.

ABSTRACT: 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.

SUBMITTER: Arimura Y

PROVIDER: S-EPMC4236741 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3.

Arimura Yasuhiro Y Shirayama Kazuyoshi K Horikoshi Naoki N Fujita Risa R Taguchi Hiroyuki H Kagawa Wataru W Fukagawa Tatsuo T Almouzni Geneviève G Kurumizaka Hitoshi H

Scientific reports 20141119

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 ...[more]

PMID: 25408271

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