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An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation
DNA methylation is an important epigenetic mark in many eukaryotes1-5. In plants, 24-nt small interfering RNAs (siRNAs) bound to the effector protein, Argonaute 4 (AGO4) can direct de novo DNA methylation by the methyltransferase DRM22,4-6. Here we report a new regulator of RNA-directed DNA methylat...
Autores principales: | , , , , , , , , , , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2865564/ https://www.ncbi.nlm.nih.gov/pubmed/20410883 http://dx.doi.org/10.1038/nature09025 |
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author | 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, Xianqiang Pontier, Dominique Lagrange, Thierry Jin, Hailing Matzke, Antonius J. Matzke, Marjori Pikaard, Craig S. Zhu, Jian-Kang |
author_facet | 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, Xianqiang Pontier, Dominique Lagrange, Thierry Jin, Hailing Matzke, Antonius J. Matzke, Marjori Pikaard, Craig S. Zhu, Jian-Kang |
author_sort | Gao, Zhihuan |
collection | PubMed |
description | DNA methylation is an important epigenetic mark in many eukaryotes1-5. In plants, 24-nt small interfering RNAs (siRNAs) bound to the effector protein, Argonaute 4 (AGO4) can direct de novo DNA methylation by the methyltransferase DRM22,4-6. 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-nt siRNAs, reduce DNA methylation, and release transcriptional gene silencing at RdDM target loci. RDM1 encodes a small protein that appears to bind single-stranded methyl DNA, and associates and co-localizes with RNA polymerase II, AGO4 and DRM2 in the nucleus. Our results suggest that RDM1 is a component of the RdDM effector complex and may play a role in linking siRNA production with pre-existing or de novo cytosine methylation. Our results also suggest that although RDM1 and Pol V may function together at some RdDM target sites in the peri-nucleolar siRNA processing center, Pol II rather than Pol V is associated with the RdDM effector complex at target sites in the nucleoplasm. |
format | Text |
id | pubmed-2865564 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
record_format | MEDLINE/PubMed |
spelling | pubmed-28655642010-11-06 An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation 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, Xianqiang Pontier, Dominique Lagrange, Thierry Jin, Hailing Matzke, Antonius J. Matzke, Marjori Pikaard, Craig S. Zhu, Jian-Kang Nature Article DNA methylation is an important epigenetic mark in many eukaryotes1-5. In plants, 24-nt small interfering RNAs (siRNAs) bound to the effector protein, Argonaute 4 (AGO4) can direct de novo DNA methylation by the methyltransferase DRM22,4-6. 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-nt siRNAs, reduce DNA methylation, and release transcriptional gene silencing at RdDM target loci. RDM1 encodes a small protein that appears to bind single-stranded methyl DNA, and associates and co-localizes with RNA polymerase II, AGO4 and DRM2 in the nucleus. Our results suggest that RDM1 is a component of the RdDM effector complex and may play a role in linking siRNA production with pre-existing or de novo cytosine methylation. Our results also suggest that although RDM1 and Pol V may function together at some RdDM target sites in the peri-nucleolar siRNA processing center, Pol II rather than Pol V is associated with the RdDM effector complex at target sites in the nucleoplasm. 2010-04-21 2010-05-06 /pmc/articles/PMC2865564/ /pubmed/20410883 http://dx.doi.org/10.1038/nature09025 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article 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, Xianqiang Pontier, Dominique Lagrange, Thierry Jin, Hailing Matzke, Antonius J. Matzke, Marjori Pikaard, Craig S. Zhu, Jian-Kang An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation |
title | An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation |
title_full | An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation |
title_fullStr | An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation |
title_full_unstemmed | An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation |
title_short | An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation |
title_sort | rna polymerase ii- and ago4-associated protein acts in rna-directed dna methylation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2865564/ https://www.ncbi.nlm.nih.gov/pubmed/20410883 http://dx.doi.org/10.1038/nature09025 |
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