PML is recruited to heterochromatin during S phase and represses DAXX-mediated histone H3.3 chromatin assembly.

Journal of Cell Science
Prashanth Krishna ShastrulaSusan M Janicki

Abstract

The incorporation of the histone H3 variant, H3.3, into chromatin by the H3.3-specific chaperone DAXX and the ATP-dependent chromatin remodeling factor ATRX is a critical mechanism for silencing repetitive DNA. DAXX and ATRX are also components of promyelocytic nuclear bodies (PML-NBs), which have been identified as sites of H3.3 chromatin assembly. Here, we use a transgene array that can be visualized in single living cells to investigate the mechanisms that recruit PML-NB proteins (i.e. PML, DAXX, ATRX, and SUMO-1, SUMO-2 and SUMO-3) to heterochromatin and their functions in H3.3 chromatin assembly. We show that DAXX and PML are recruited to the array through distinct SUMOylation-dependent mechanisms. Additionally, PML is recruited during S phase and its depletion increases H3.3 deposition. Since this effect is abrogated when PML and DAXX are co-depleted, it is likely that PML represses DAXX-mediated H3.3 chromatin assembly. Taken together, these results suggest that, at heterochromatin, PML-NBs coordinate H3.3 chromatin assembly with DNA replication, which has important implications for understanding how transcriptional silencing is established and maintained.

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Citations

Aug 17, 2019·Cells·Anna LångStig Ove Bøe
Jul 28, 2019·Nucleic Acids Research·Iqbal Mahmud, Daiqing Liao
Oct 18, 2020·Nucleic Acids Research·Armelle CorpetPatrick Lomonte
Feb 3, 2021·International Journal of Molecular Sciences·Irina Bogolyubova, Dmitry Bogolyubov
Feb 19, 2021·Frontiers in Cellular and Infection Microbiology·Mila Collados Rodríguez
Jun 13, 2020·Trends in Cancer·Yuwen LiGuoyu Meng

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