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Title | CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation. |
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Journal, issue, pages | Nat Commun, Vol. 10, Issue 1, Page 3916, Year 2019 |
Publish date | Sep 2, 2019 |
Authors | Somsakul Pop Wongpalee / Shiheng Liu / Javier Gallego-Bartolomé / Alexander Leitner / Ruedi Aebersold / Wanlu Liu / Linda Yen / Maria A Nohales / Peggy Hsuanyu Kuo / Ajay A Vashisht / James A Wohlschlegel / Suhua Feng / Steve A Kay / Z Hong Zhou / Steven E Jacobsen / |
PubMed 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 ...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. |
External links | Nat Commun / PubMed:31477705 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.5 - 3.6 Å |
Structure data | EMDB-20080, PDB-6ois: EMDB-20081, PDB-6oit: |
Source |
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Keywords | PLANT PROTEIN / SMC-hinge / Coiled-coil / SNF2 / RNA-directed DNA methylation |