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CryoEM structures of Arabidopsis DDR complexes involved in RNA-directed DNA methylation.

Nat Commun. 2019 Sep 02;10(1):3916
Somsakul Pop Wongpalee 1 , Shiheng Liu 2 , Javier Gallego-Bartolomé 3 , Alexander Leitner 4 , Ruedi Aebersold 5 , Wanlu Liu 6 , Linda Yen 3 , Maria A Nohales 7 , Peggy Hsuanyu Kuo 3 , Ajay A Vashisht 8 , James A Wohlschlegel 8 , Suhua Feng 3 , Steve A Kay 7 , Z Hong Zhou 9 , Steven E Jacobsen 10
Somsakul Pop Wongpalee 1 , Shiheng Liu 2 , Javier Gallego-Bartolomé 3 , Alexander Leitner 4 , Ruedi Aebersold 5 , Wanlu Liu 6 , Linda Yen 3 , Maria A Nohales 7 , Peggy Hsuanyu Kuo 3 , Ajay A Vashisht 8 , James A Wohlschlegel 8 , Suhua Feng 3 , Steve A Kay 7 , Z Hong Zhou 9 , Steven E Jacobsen 10
+ et al

[No authors listed]

Author information
  • 1 Department of Microbiology, Faculty of Medicine, Chiang Mai University, Chiang Mai, 50200, Thailand.
  • 2 California NanoSystems Institute (CNSI), UCLA, Los Angeles, CA, 90095, USA.
  • 3 Department of Molecular, Cellular and Developmental Biology, University of California, Los Angeles (UCLA), Los Angeles, CA, 90095, USA.
  • 4 Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, 8093, Zürich, Switzerland.
  • 5 Faculty of Science, University of Zürich, 8057, Zürich, Switzerland.
  • 6 Zhejiang University-University of Edinburgh Institute, Zhejiang University School of Medicine, 310058, Hangzhou, P. R. China.
  • 7 Keck School of Medicine, University of Southern California, Los Angeles, CA, 90089, USA.
  • 8 Department of Biological Chemistry, UCLA, Los Angeles, CA, 90095, USA.
  • 9 California NanoSystems Institute (CNSI), UCLA, Los Angeles, CA, 90095, USA. hong.zhou@ucla.edu.
  • 10 Howard Hughes Medical Institute (HHMI), UCLA, Los Angeles, CA, 90095, USA. jacobsen@ucla.edu.

摘要

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.

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