Journal
CELL
Volume 157, Issue 5, Pages 1050-1060Publisher
CELL PRESS
DOI: 10.1016/j.cell.2014.03.056
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Funding
- Ruth L. Kirschstein National Research Service Award [F32GM096483-01]
- Frontiers Science Program [LT000425/2012-L]
- Abby Rockefeller Mauze Trust
- Maloris foundation
- STARR foundation
- NIH [GM60398, GM094428]
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DNA methylation is a conserved epigenetic generegulation mechanism. DOMAINS REARRANGED METHYLTRANSFERASE (DRM) is a key de novo methyltransferase in plants, but how DRM acts mechanistically is poorly understood. Here, we report the crystal structure of the methyltransferase domain of tobacco DRM (NtDRM) and reveal a molecular basis for its rearranged structure. NtDRM forms a functional homodimer critical for catalytic activity. We also show that Arabidopsis DRM2 exists in complex with the small interfering RNA (siRNA) effector ARGONAUTE4 (AGO4) and preferentially methylates one DNA strand, likely the strand acting as the template for RNA polymerase V- mediated noncoding RNA transcripts. This strand- biased DNA methylation is also positively correlated with strand- biased siRNA accumulation. These data suggest a model in which DRM2 is guided to target loci by AGO4- siRNA and involves base-pairing of associated siRNAs with nascent RNA transcripts.
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