EMD-20080
CryoEM structure of Arabidopsis DR complex (DMS3-RDM1)
EMD-20080
Single-particle3.6 Å
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Map released: 24/07/2019
Last modified: 20/03/2024
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
Sample: DR complex of DMS3 with RDM1
Fitted models: 6ois (Avg. Q-score: 0.444)
Deposition Authors: Wongpalee SP
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CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation.
Wongpalee SP
,
Liu S
,
Gallego-Bartolome J
,
Leitner A
,
Aebersold R
,
Liu W,
Yen L,
Nohales MA
,
Kuo PH,
Vashisht AA,
Wohlschlegel JA,
Feng S,
Kay SA,
Zhou ZH
,
Jacobsen SE
(2019) Nat Commun , 10 , 3916 - 3916
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(2019) Nat Commun , 10 , 3916 - 3916
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.
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.