EMD-20080

Single-particle
3.6 Å
EMD-20080 Deposition: 09/04/2019
Map released: 24/07/2019
Last modified: 20/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-20080

CryoEM structure of Arabidopsis DR complex (DMS3-RDM1)

EMD-20080

Single-particle
3.6 Å
EMD-20080 Deposition: 09/04/2019
Map released: 24/07/2019
Last modified: 20/03/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Arabidopsis thaliana
Sample: DR complex of DMS3 with RDM1
Fitted models: 6ois (Avg. Q-score: 0.444)

Deposition Authors: Wongpalee SP , Liu S
CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation.
PUBMED: 31477705
DOI: doi:10.1038/s41467-019-11759-9
ISSN: 2041-1723
Abstract:
Transcription by RNA polymerase V (Pol V) in plants is required for RNA-directed DNA methylation, leading to transcriptional gene silencing. Global chromatin association of Pol V requires components of the DDR complex DRD1, DMS3 and RDM1, but the assembly process of this complex and the underlying mechanism for Pol V recruitment remain unknown. Here we show that all DDR complex components co-localize with Pol V, and we report the cryoEM structures of two complexes associated with Pol V recruitment-DR (DMS3-RDM1) and DDR' (DMS3-RDM1-DRD1 peptide), at 3.6 Å and 3.5 Å resolution, respectively. RDM1 dimerization at the center frames the assembly of the entire complex and mediates interactions between DMS3 and DRD1 with a stoichiometry of 1 DRD1:4 DMS3:2 RDM1. DRD1 binding to the DR complex induces a drastic movement of a DMS3 coiled-coil helix bundle. We hypothesize that both complexes are functional intermediates that mediate Pol V recruitment.