The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Molecular Mechanism of Action of Plant DRM De Novo DNA Methyltransferases
Open accessAbstract
SUMMARY DNA methylation is a conserved epigenetic gene regulation 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 homo-dimer critical for catalytic activity. We also show that Arabidopsis DRM2 exists in complex with the siRNA effector ARGONAUTE4 (AGO4) and preferentially methylates one DNA strand, likely the strand acting as the template for RNA polymerase V mediated non-coding 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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Metadata
- Authors
- Zhong, X., Du, J., Hale, C. J., Gallego-Bartolome, J., Feng, S., Vashisht, A. A., Chory, J., Wohlschlegel, J. A., Patel, D. J., & Jacobsen, S. E.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2014-05
- Volume
- 157
- Issue
- 5
- Pages
- 1050-1060
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2029687716
- Cited by
- 320
- References
- 37
- FWCI
- 9.86
- Type
- journal article
- Language
- en
- Open access
- bronze
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