Molecular mechanism of action of plant DRM de novo DNA methyltransferases Journal Article
| 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. |
| Article Title: | Molecular mechanism of action of plant DRM de novo DNA methyltransferases |
| Abstract: | 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 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. © 2014 Elsevier Inc. |
| Keywords: | controlled study; unclassified drug; nonhuman; enzyme inhibition; small interfering rna; enzyme activity; dna methylation; base pairing; crystal structure; dimerization; untranslated rna; tobacco; dna methyltransferase; enzyme structure; enzyme active site; rna polymerase; plant; arabidopsis; dna template; nucleic acid binding protein; dna strand; homodimer; priority journal; article; argonaute 4 protein; domains rearranged methyltransferase |
| Journal Title: | Cell |
| Volume: | 157 |
| Issue: | 5 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 2014-05-22 |
| Start Page: | 1050 |
| End Page: | 1060 |
| Language: | English |
| DOI: | 10.1016/j.cell.2014.03.056 |
| PROVIDER: | scopus |
| PUBMED: | 24855943 |
| PMCID: | PMC4123750 |
| DOI/URL: | |
| Notes: | Cell -- Export Date: 8 July 2014 -- CODEN: CELLB -- Source: Scopus |
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