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RESEARCH COMMUNICATION
1 Laboratoire Génome et Développement de Plantes, Centre National de la Recherche Scientifique/Institut de Recherche pour le Développement/Université de Perpignan 5096, 66860 Perpignan Cedex, France; 2 Institut Jean Roget, Université Joseph Fourier, BP170, 38042 Grenoble Cedex 9, France; 3 Department of Molecular, Cell and Developmental Biology, Howard Hughes Medical Institute, University of California at Los Angeles, Los Angeles, California 90095, USA
Two forms of RNA Polymerase IV (PolIVa/PolIVb) have been implicated in RNA-directed DNA methylation (RdDM) in Arabidopsis. Prevailing models imply a distinct function for PolIVb by association of Argonaute4 (AGO4) with the C-terminal domain (CTD) of its largest subunit NRPD1b. Here we show that the extended CTD of NRPD1b-type proteins exhibits conserved Argonaute-binding capacity through a WG/GW-rich region that functionally distinguishes Pol IVb from Pol IVa, and that is essential for RdDM. Site-specific mutagenesis and domain-swapping experiments between AtNRPD1b and the human protein GW182 demonstrated that reiterated WG/GW motifs form evolutionarily and functionally conserved Argonaute-binding platforms in RNA interference (RNAi)-related components.
[Keywords: RNAPIV; CTD; WG/GW motifs, Argonaute; RNA silencing]
Received July 30, 2007; revised version accepted August 30, 2007.
E-MAIL lagrange{at}univ-perp.fr; FAX 33-468668499.
Supplemental material is available at http://www.genesdev.org.
Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.451207
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