Reiterated WG/GW motifs form functionally and evolutionarily conserved ARGONAUTE-binding platforms in RNAi-related components.
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.
Mesh Terms:
Amino Acid Motifs, Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Conserved Sequence, DNA Methylation, DNA-Directed RNA Polymerases, Evolution, Molecular, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Plants, Genetically Modified, Protein Binding, Protein Structure, Tertiary, Protein Subunits, RNA Interference, Repetitive Sequences, Amino Acid, Sequence Homology, Amino Acid
Amino Acid Motifs, Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Conserved Sequence, DNA Methylation, DNA-Directed RNA Polymerases, Evolution, Molecular, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Plants, Genetically Modified, Protein Binding, Protein Structure, Tertiary, Protein Subunits, RNA Interference, Repetitive Sequences, Amino Acid, Sequence Homology, Amino Acid
Genes Dev.
Date: Oct. 15, 2007
PubMed ID: 17938239
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