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An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation.

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Gao, Zhihuan | Liu, Hai-Liang | Daxinger, Lucia | Pontes, Olga | He, Xinjian | Qian, Weiqiang | Lin, Huixin | Xie, Mingtang | Lorkovic, Zdravko J | Zhang, Shoudong | Miki, Daisuke | Zhan, Xiangqiang | Pontier, Dominique | Lagrange, Thierry | Jin, Hailing | Matzke, Antonius J M | Matzke, Marjori | Pikaard, Craig S | Zhu, Jian-Kang

Edité par CCSD ; Nature Publishing Group -

International audience. 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.

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