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A cryo-EM structure of KTF1-bound polymerase V transcription elongation complex

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  • Hong-Wei Zhang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Kun Huang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Zhan-Xi Gu

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Xiao-Xian Wu

    (Chinese Academy of Sciences)

  • Jia-Wei Wang

    (Chinese Academy of Sciences)

  • Yu Zhang

    (Chinese Academy of Sciences)

Abstract

De novo DNA methylation in plants relies on transcription of RNA polymerase V (Pol V) along with KTF1, which produce long non-coding RNAs for recruitment and assembly of the DNA methylation machinery. Here, we report a cryo-EM structure of the Pol V transcription elongation complex bound to KTF1. The structure reveals the conformation of the structural motifs in the active site of Pol V that accounts for its inferior RNA-extension ability. The structure also reveals structural features of Pol V that prevent it from interacting with the transcription factors of Pol II and Pol IV. The KOW5 domain of KTF1 binds near the RNA exit channel of Pol V providing a scaffold for the proposed recruitment of Argonaute proteins to initiate the assembly of the DNA methylation machinery. The structure provides insight into the Pol V transcription elongation process and the role of KTF1 during Pol V transcription-coupled DNA methylation.

Suggested Citation

  • Hong-Wei Zhang & Kun Huang & Zhan-Xi Gu & Xiao-Xian Wu & Jia-Wei Wang & Yu Zhang, 2023. "A cryo-EM structure of KTF1-bound polymerase V transcription elongation complex," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-38619-x
    DOI: 10.1038/s41467-023-38619-x
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    References listed on IDEAS

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