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

Hong-Wei Zhang, Kun Huang, Zhan-Xi Gu, Xiao-Xian Wu, Jia-Wei Wang and Yu Zhang ()
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Hong-Wei Zhang: Chinese Academy of Sciences
Kun Huang: Chinese Academy of Sciences
Zhan-Xi Gu: Chinese Academy of Sciences
Xiao-Xian Wu: Chinese Academy of Sciences
Jia-Wei Wang: Chinese Academy of Sciences
Yu Zhang: Chinese Academy of Sciences

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-38619-x

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