Skip to Main content Skip to Navigation
Journal articles

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

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.
Complete list of metadata
Contributor : Elisabeth Goetschy Connect in order to contact the contributor
Submitted on : Thursday, February 14, 2013 - 2:13:29 PM
Last modification on : Friday, May 6, 2022 - 2:54:40 PM

Links full text




Zhihuan Gao, Hai-Liang Liu, Lucia Daxinger, Olga Pontes, Xinjian He, et al.. An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation.. Nature, Nature Publishing Group, 2010, 465 (7294), pp.106-9. ⟨10.1038/nature09025⟩. ⟨hal-00788419⟩



Record views