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SWI2/SNF2 ATPase CHR2 remodels pri-miRNAs via Serrate to impede miRNA production

Author

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  • Zhiye Wang

    (Texas A&M University
    Institute for Plant Genomics and Biotechnology, Texas A&M University)

  • Zeyang Ma

    (Texas A&M University
    Institute for Plant Genomics and Biotechnology, Texas A&M University)

  • Claudia Castillo-González

    (Texas A&M University
    Institute for Plant Genomics and Biotechnology, Texas A&M University)

  • Di Sun

    (Texas A&M University
    Institute for Plant Genomics and Biotechnology, Texas A&M University)

  • Yanjun Li

    (Texas A&M University
    Institute for Plant Genomics and Biotechnology, Texas A&M University
    Nanjing Agricultural University)

  • Bin Yu

    (University of Nebraska-Lincoln)

  • Baoyu Zhao

    (Texas A&M University)

  • Pingwei Li

    (Texas A&M University)

  • Xiuren Zhang

    (Texas A&M University
    Institute for Plant Genomics and Biotechnology, Texas A&M University)

Abstract

Chromatin remodelling factors (CHRs) typically function to alter chromatin structure. CHRs also reside in ribonucleoprotein complexes, but little is known about their RNA-related functions. Here we show that CHR2 (also known as BRM), the ATPase subunit of the large switch/sucrose non-fermentable (SWI/SNF) complex, is a partner of the Microprocessor component Serrate (SE). CHR2 promotes the transcription of primary microRNA precursors (pri-miRNAs) while repressing miRNA accumulation in vivo. Direct interaction with SE is required for post-transcriptional inhibition of miRNA accumulation by CHR2 but not for its transcriptional activity. CHR2 can directly bind to and unwind pri-miRNAs and inhibit their processing, and this inhibition requires the remodelling and helicase activity of CHR2 in vitro and in vivo. Furthermore, the secondary structures of pri-miRNAs differed between wild-type Arabidopsis thaliana and chr2 mutants. We conclude that CHR2 accesses pri-miRNAs through SE and remodels their secondary structures, preventing downstream processing by DCL1 and HYL1. Our study uncovers pri-miRNAs as a substrate of CHR2, and an additional regulatory layer upstream of Microprocessor activity to control miRNA accumulation.

Suggested Citation

  • Zhiye Wang & Zeyang Ma & Claudia Castillo-González & Di Sun & Yanjun Li & Bin Yu & Baoyu Zhao & Pingwei Li & Xiuren Zhang, 2018. "SWI2/SNF2 ATPase CHR2 remodels pri-miRNAs via Serrate to impede miRNA production," Nature, Nature, vol. 557(7706), pages 516-521, May.
    • Handle: RePEc:nat:nature:v:557:y:2018:i:7706:d:10.1038_s41586-018-0135-x
    DOI: 10.1038/s41586-018-0135-x
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    Cited by:

    1. Chao Liang & Qiang Cai & Fei Wang & Shaofang Li & Chenjiang You & Chi Xu & Lei Gao & Dechang Cao & Ting Lan & Bailong Zhang & Beixin Mo & Xuemei Chen, 2022. "Arabidopsis RBV is a conserved WD40 repeat protein that promotes microRNA biogenesis and ARGONAUTE1 loading," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Dong Zhang & Lulu Qiao & Xiaobo Lei & Xiaojing Dong & Yunguang Tong & Jianwei Wang & Zhiye Wang & Ruhong Zhou, 2023. "Mutagenesis and structural studies reveal the basis for the specific binding of SARS-CoV-2 SL3 RNA element with human TIA1 protein," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Bangjun Zhou & Huihui Yu & Yong Xue & Mu Li & Chi Zhang & Bin Yu, 2024. "The spliceosome-associated protein CWC15 promotes miRNA biogenesis in Arabidopsis," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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