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. Author manuscript; available in PMC: 2010 May 1.
Published in final edited form as: Cell. 2009 May 1;137(3):498–508. doi: 10.1016/j.cell.2009.04.028

Figure 4. The WG/GW repeats in KTF1 C-terminal domain interact with AGO4.

Figure 4

(A) KTF1, NRPE1, HsGW182 and proteins are shown schematically. All three proteins are characterized by the reiterated WG/GW repeats-containing domains (in yellow). The red stripes represent each of the WG/GW repeat. WG-1 and WG-2 represent two highly conserved WG repeat regions in KTF1. (B) Diagram of the bacterially expressed NRPE1-CTD and truncated KTF1 proteins. (C) The purified proteins were subjected to SDS-PAGE and gels were stained with Coomassie. Arrows point to the proteins of interest. (D) Western blot analysis showing that the GST-fused truncated KTF1 and NRPE1-CTD interact with Myc-AGO4 from plant extracts. Ten percent of the input was used in the “Input” lane. (E) Anti-Myc antibody-conjugated beads captured truncated KTF1 proteins and NRPE1-CTD from a mixture of the proteins with extract from Myc-AGO4 plants. Arrows point to the proteins of interest. (F) and (G) Western blot analysis showing coimmunoprecipitation of KTF1 and Myc-AGO4. Ler wild-type plants without the Myc-AGO4 transgene were used as controls. No AB, control precipitation without using antibodies.