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-Structure paper
Title | A cryo-EM structure of KTF1-bound polymerase V transcription elongation complex. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 3118, Year 2023 |
Publish date | May 30, 2023 |
Authors | Hong-Wei Zhang / Kun Huang / Zhan-Xi Gu / Xiao-Xian Wu / Jia-Wei Wang / Yu Zhang / |
PubMed 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. ...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. |
External links | Nat Commun / PubMed:37253723 / PubMed Central |
Methods | EM (single particle) |
Resolution | 4.3 Å |
Structure data | EMDB-35086, PDB-8hyj: |
Chemicals | ChemComp-MG: ChemComp-ZN: |
Source |
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Keywords | TRANSCRIPTION / Pol V |