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Fig. 6. RNF17 binds to itself both in vivo and in vitro. (A) Identification of the RNF17 granule formation domain. Truncated RNF17 polypeptides were expressed as GFP fusion proteins in NIH 3T3 cells. Formation of granules was assayed by fluorescence microscopy. +, formation of GFP-RNF17 granules; -, diffuse GFP-RNF17 distribution. The numbers adjacent to the endpoints designate the corresponding amino acid positions. (B) Distribution of GFP-fusion proteins expressed in NIH 3T3 cells. Punctate granules were present in cells expressing RNF17L (1-1640), RNF17S (1-1130), RNF17 (1-626), RNF17 (1-287) or RNF17 (243-287). RNF17 (286-626) or GFP alone (data not shown) was diffusely distributed. (C) Co-immunoprecipitation of RNF17L and RNF17S from testis. Immunoprecipitation (IP) using testis protein extracts was carried out with RNF17L-specific antibodies (anti-serum GP8). Immunoprecipitated proteins were subjected to western blot analysis with anti-serum 1774. IP with pre-bleed serum served as a control. (D) GST-pulldown assay. GST-RNF17 (1-287) was expressed in E. coli and purified with glutathione beads. RNF17 (1-626) was in vitro translated in the presence of [³⁵S]methionine. GST alone served as a control.

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