8HYJ

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

Summary for 8HYJ

• Entry DOI: 10.2210/pdb8hyj/pdb
• EMDB information: 35086
• Descriptor: DNA-directed RNA polymerase V subunit 1, DNA-directed RNA polymerases II, IV and V subunit 10, DNA-directed RNA polymerases II, IV and V subunit 11, ... (18 entities in total)
• Functional Keywords: pol v, transcription
• Biological source: Arabidopsis thaliana (thale cress); More
• Total number of polymer chains: 16
• Total formula weight: 727238.03

Authors

Zhang, H.,Zhang, Y. (deposition date: 2023-01-06, release date: 2023-06-21, Last modification date: 2024-05-29)

Primary citation

Zhang, H.W.,Huang, K.,Gu, Z.X.,Wu, X.X.,Wang, J.W.,Zhang, Y.
A cryo-EM structure of KTF1-bound polymerase V transcription elongation complex.
Nat Commun, 14:3118-3118, 2023

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. 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.

PubMed: 37253723
DOI: 10.1038/s41467-023-38619-x

Experimental method

ELECTRON MICROSCOPY (4.3 Å)