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- Title
An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation.
- Authors
Zhihuan Gao; Hai-Liang Liu; Daxinger, Lucia; Pontes, Olga; Xinjian He; Weiqiang Qian; Huixin Lin; Mingtang Xie; Lorkovic, Zdravko J.; Shoudong Zhang; Miki, Daisuke; Xiangqiang Zhan; Pontier, Dominique; Lagrange, Thierry; Jin, Hailing; Matzke, Antonius J. M.; Matzke, Marjori; Pikaard, Craig S.; Jian-Kang Zhu
- Abstract
DNA methylation is an important epigenetic mark in many eukaryotes. In plants, 24-nucleotide small interfering RNAs (siRNAs) bound to the effector protein, Argonaute 4 (AGO4), can direct de novo DNA methylation by the methyltransferase DRM2 (refs 2, 4–6). Here we report a new regulator of RNA-directed DNA methylation (RdDM) in Arabidopsis: RDM1. Loss-of-function mutations in the RDM1 gene impair the accumulation of 24-nucleotide siRNAs, reduce DNA methylation, and release transcriptional gene silencing at RdDM target loci. RDM1 encodes a small protein that seems to bind single-stranded methyl DNA, and associates and co-localizes with RNA polymerase II (Pol II, also known as NRPB), AGO4 and DRM2 in the nucleus. Our results indicate that RDM1 is a component of the RdDM effector complex and may have a role in linking siRNA production with pre-existing or de novo cytosine methylation. Our results also indicate that, although RDM1 and Pol V (also known as NRPE) may function together at some RdDM target sites in the peri-nucleolar siRNA processing centre, Pol II rather than Pol V is associated with the RdDM effector complex at target sites in the nucleoplasm.
- Publication
Nature, 2010, Vol 465, Issue 7294, p106
- ISSN
0028-0836
- Publication type
Academic Journal
- DOI
10.1038/nature09025