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. 2010 Mar 24;38(13):4231–4245. doi: 10.1093/nar/gkq162

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© The Author(s) 2010. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — WGRP1 protein has Argonaute-binding capacity. (A) Primary sequence of the Arabidopsis WGRP1 sequence. The evolutionarily conserved N-terminal sequence is bolded and the location of the intron relative to the open reading frame is indicated by a vertical arrowhead. The WG/GW motifs in the WGRP1 CTD are in red and the WGRP1 sequence fused to GST is underlined. (B) Coomassie staining of the purified GST and GST-WGRP1 recombinant proteins used in the Argonaute-binding assay. (C) Preferential binding of AGO4 to the WG/GW-rich domain of WGRP1 protein. Myc-AGO4 or Flag-AGO1 extracts were applied to equimolar amounts of GST and GST-based fusion protein beads and the bound protein (Pellet) and supernatant (Super) fractions detected by immunoblotting with anti-Myc or anti-M2 antibodies. The GST protein was used as control.