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dc.contributor.authorGao, Zhihuan
dc.contributor.authorLiu, Hai-Liang
dc.contributor.authorDaxinger, Lucia
dc.contributor.authorPontes, Olga
dc.contributor.authorHe, Xinjian
dc.contributor.authorQian, Weiqiang
dc.contributor.authorLin, Huixin
dc.contributor.authorXie, Mingtang
dc.contributor.authorLorkovic, Zdravko J.
dc.contributor.authorZhang, ShouDong
dc.contributor.authorMiki, Daisuke
dc.contributor.authorZhan, Xiangqiang
dc.contributor.authorPontier, Dominique
dc.contributor.authorLagrange, Thierry
dc.contributor.authorJin, Hailing
dc.contributor.authorMatzke, Antonius J.
dc.contributor.authorMatzke, Marjori
dc.contributor.authorPikaard, Craig S.
dc.contributor.authorZhu, Jian-Kang
dc.date.accessioned2014-08-27T09:45:15Z
dc.date.available2014-08-27T09:45:15Z
dc.date.issued2010-04-21
dc.identifier.citationGao Z, Liu H-L, Daxinger L, Pontes O, He X, et al. (2010) An RNA polymerase II- and AGO4-associated protein acts in RNA-directed DNA methylation. Nature 465: 106-109. doi:10.1038/nature09025.
dc.identifier.issn00280836
dc.identifier.pmid20410883
dc.identifier.doi10.1038/nature09025
dc.identifier.urihttp://hdl.handle.net/10754/325291
dc.description.abstractDNA 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. © 2010 Macmillan Publishers Limited. All rights reserved.
dc.language.isoen
dc.publisherSpringer Nature
dc.rightsUsers 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
dc.rightsArchived with thanks to Nature
dc.subjectargonaute protein
dc.subjectcytosine
dc.subjectmethyltransferase
dc.subjectnucleotide
dc.subjectRNA polymerase II
dc.subjectsingle stranded DNA
dc.subjectsmall interfering RNA
dc.subjectenzyme
dc.subjecteukaryote
dc.subjectgenetic marker
dc.subjectherb
dc.subjectmethylation
dc.subjectmutation
dc.subjectnucleic acid
dc.subjectpolymerase chain reaction
dc.subjectprotein
dc.subjectArabidopsis
dc.subjectcontrolled study
dc.subjectDNA methylation
dc.subjectDNA RNA hybridization
dc.subjectgene locus
dc.subjectgene silencing
dc.subjectloss of function mutation
dc.subjectprotein DNA binding
dc.subjectprotein function
dc.subjectRNA processing
dc.subjectArabidopsis
dc.subjectArabidopsis Proteins
dc.subjectCell Nucleus
dc.subjectDNA Methylation
dc.subjectDNA-Binding Proteins
dc.subjectGene Expression Regulation, Plant
dc.subjectGene Silencing
dc.subjectMethyltransferases
dc.subjectMutation
dc.subjectRNA Polymerase II
dc.subjectRNA, Plant
dc.subjectArabidopsis
dc.subjectEukaryota
dc.titleAn RNA polymerase II-and AGO4-associated protein acts in RNA-directed DNA methylation
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentDesert Agriculture Initiative
dc.contributor.departmentOffice of the VP
dc.contributor.departmentPlant Stress Genomics Research Lab
dc.identifier.journalNature
dc.identifier.pmcidPMC2865564
dc.eprint.versionPost-print
dc.contributor.institutionInstitute for Integrative Genome Biology, Department of Botany and Plant Sciences, University of California, Riverside, CA 92521, United States
dc.contributor.institutionSchool of Life Science and Technology, Tongji University, Shanghai 200092, China
dc.contributor.institutionGregor Mendel Institute of Molecular Plant Biology, Austrian Academy of Sciences, 1030 Vienna, Austria
dc.contributor.institutionBiology Department, Washington University, St Louis, MI 63130, United States
dc.contributor.institutionMax F. Perutz Laboratory, Medical University of Vienna, 1030 Vienna, Austria
dc.contributor.institutionLGDP, CNRS/IRD/Université de Perpignan, UMR 5096, 66860 Perpignan, France
dc.contributor.institutionInstitute for Integrative Genome Biology, Department of Plant Pathology and Microbiology, University of California, Riverside, CA 92521, United States
dc.contributor.institutionDepartment of Biology, Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN 47405, United States
dc.contributor.institutionDivision of Genetics and Population Health, Queensland Institute of Medical Research, QLD 4006, Herston, Australia
dc.contributor.affiliationKing Abdullah University of Science and Technology (KAUST)
kaust.personHe, Xinjian
kaust.personZhang, ShouDong
kaust.personZhan, Xiangqiang
kaust.personZhu, Jian-Kang
refterms.dateFOA2018-06-14T03:38:44Z
dc.date.published-online2010-04-21
dc.date.published-print2010-05


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