CENP-B protects centromere chromatin integrity by facilitating histone deposition via the H3.3-specific chaperone Daxx.

ABSTRACT:

Background

The main chromatin unit, the nucleosome, can be modulated by the incorporation of histone variants that, in combination with posttranslational histones modifications, determine epigenetics properties of chromatin. Understanding the mechanism that creates a histone variants landscape at different genomic elements is expected to elevate our comprehension of chromatin assembly and function. The Daxx chaperone deposits transcription-associated histone H3.3 at centromeres, but mechanism of centromere-specific Daxx targeting remains unclear.

Results

In this study, we identified an unexpected function of the constitutive centromeric protein CENP-B that serves as a "beacon" for H3.3 incorporation. CENP-B depletion reduces Daxx association and H3.3 incorporation at centrom

SUBMITTER: Morozov VM 

PROVIDER: S-EPMC5741900 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature