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TitleA cryo-EM structure of KTF1-bound polymerase V transcription elongation complex.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 3118, Year 2023
Publish dateMay 30, 2023
AuthorsHong-Wei Zhang / Kun Huang / Zhan-Xi Gu / Xiao-Xian Wu / Jia-Wei Wang / Yu Zhang /
PubMed AbstractDe 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 linksNat Commun / PubMed:37253723 / PubMed Central
MethodsEM (single particle)
Resolution4.3 Å
Structure data

35086

8hyj

EMDB-35086, PDB-8hyj:
A cryo-EM structure of KTF1-bound polymerase V transcription elongation complex
Method: EM (single particle) / Resolution: 4.3 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • arabidopsis thaliana (thale cress)
  • synthetic construct (others)
KeywordsTRANSCRIPTION / Pol V

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