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The repressive role of Arabidopsis H2A.Z in transcriptional regulation depends on AtBMI1 activity

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  • Ángeles Gómez-Zambrano

    (Institute of Plant Biochemistry and Photosynthesis (IBVF-CSIC-University of Seville))

  • Wiam Merini

    (Institute of Plant Biochemistry and Photosynthesis (IBVF-CSIC-University of Seville))

  • Myriam Calonje

    (Institute of Plant Biochemistry and Photosynthesis (IBVF-CSIC-University of Seville))

Abstract

H2A.Z variant has emerged as a critical player in regulating plant responses to environment; however, the mechanism by which H2A.Z mediates this regulation remains unclear. In Arabidopsis, H2A.Z has been proposed to have opposite effects on transcription depending on its localization within the gene. These opposite roles have been assigned by correlating gene expression and H2A.Z enrichment analyses but without considering the impact of possible H2A.Z post-translational modifications. Here, we show that H2A.Z can be monoubiquitinated by the PRC1 components AtBMI1A/B/C. The incorporation of this modification is required for H2A.Z-mediated transcriptional repression through a mechanism that does not require PRC2 activity. Our data suggest that the dual role of H2A.Z in regulating gene expression depends on the modification that it carries, while the levels of H2A.Z within genes depend on the transcriptional activity.

Suggested Citation

  • Ángeles Gómez-Zambrano & Wiam Merini & Myriam Calonje, 2019. "The repressive role of Arabidopsis H2A.Z in transcriptional regulation depends on AtBMI1 activity," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10773-1
    DOI: 10.1038/s41467-019-10773-1
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    Cited by:

    1. Lorna A. Farrelly & Shuangping Zheng & Nadine Schrode & Aaron Topol & Natarajan V. Bhanu & Ryan M. Bastle & Aarthi Ramakrishnan & Jennifer C Chan & Bulent Cetin & Erin Flaherty & Li Shen & Kelly Gleas, 2022. "Chromatin profiling in human neurons reveals aberrant roles for histone acetylation and BET family proteins in schizophrenia," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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