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Arabidopsis γ-H2A.X-INTERACTING PROTEIN participates in DNA damage response and safeguards chromatin stability

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  • Tianyi Fan

    (Fudan University)

  • Huijia Kang

    (Fudan University
    Fudan University)

  • Di Wu

    (Fudan University)

  • Xinyu Zhu

    (Tsinghua University)

  • Lin Huang

    (Fudan University)

  • Jiabing Wu

    (Fudan University)

  • Yan Zhu

    (Fudan University)

Abstract

Upon the occurrence of DNA double strand breaks (DSB), the proximal histone variant H2A.X is phosphorylated as γ-H2A.X, a critical signal for consequent DSB signaling and repair pathways. Although γ-H2A.X-triggered DNA damage response (DDR) has been well-characterized in yeast and animals, the corresponding pathways in plant DDR are less well understood. Here, we show that an Arabidopsis protein γ-H2A.X-INTERACTING PROTEIN (XIP) can interact with γ-H2A.X. Its C-terminal dual-BRCT-like domain contributes to its specific interaction with γ-H2A.X. XIP-deficient seedlings display smaller meristems, inhibited growth, and higher sensitivity to DSB-inducing treatment. Loss-of-function in XIP causes transcriptome changes mimicking wild-type plants subject to replicative or genotoxic stresses. After genotoxic bleomycin treatment, more proteins with upregulated phosphorylation modifications, more DNA fragments and cell death were found in xip mutants. Moreover, XIP physically interacts with RAD51, the key recombinase in homologous recombination (HR), and somatic HR frequency is significantly reduced in xip mutants. Collectively, XIP participates in plant response to DSB and contributes to chromatin stability.

Suggested Citation

  • Tianyi Fan & Huijia Kang & Di Wu & Xinyu Zhu & Lin Huang & Jiabing Wu & Yan Zhu, 2022. "Arabidopsis γ-H2A.X-INTERACTING PROTEIN participates in DNA damage response and safeguards chromatin stability," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-35715-2
    DOI: 10.1038/s41467-022-35715-2
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    References listed on IDEAS

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    1. Zhenkun Lou & Katherine Minter-Dykhouse & Xianglin Wu & Junjie Chen, 2003. "MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways," Nature, Nature, vol. 421(6926), pages 957-961, February.
    2. Grant S. Stewart & Bin Wang & Colin R. Bignell & A. Malcolm R. Taylor & Stephen J. Elledge, 2003. "MDC1 is a mediator of the mammalian DNA damage checkpoint," Nature, Nature, vol. 421(6926), pages 961-966, February.
    3. Kangxi Du & Qiang Luo & Liufan Yin & Jiabing Wu & Yuhao Liu & Jianhua Gan & Aiwu Dong & Wen-Hui Shen, 2020. "OsChz1 acts as a histone chaperone in modulating chromatin organization and genome function in rice," Nature Communications, Nature, vol. 11(1), pages 1-17, December.
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