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Fig. 1. Molecular interactions between Hairless and Pros26.4. (A) Schematic drawing of Hairless deletion constructs. HFL, full-length Hairless (1076 aa), with SBD, Suppressor-of-Hairless-binding domain; GBD, Groucho-binding domain; CBD, binding site of the C-terminal binding protein CtBP. C1, N-terminal truncation (929 aa); C2, deletion of the Su(H)-binding domain (H ${Delta}$ S; 885 aa); C3, deletion of acidic domain (867 aa); CX, internal deletion within the C-terminal third of the Hairless protein (751 aa); C6, C-terminal truncation of 15 amino acids including the CtBP-binding domain (H ${Delta}$ C; 1061 aa) [compare with Maier et al. (Maier et al., 1997)]. (B) Quantification of the interaction of Pros26.4 (pJG-S4) with Hairless and its deletion constructs. The quantitative yeast two-hybrid assay shows that the Hairless full-length construct (HFL) as well as all Hairless deletion constructs, with the exception of CX, retain interaction capacity. Control was empty vector (pEG). Values represent Miller units. (C) Drawing of Pros26.4 protein; the conserved AAA-ATPase domain (AAA) is located in the C-terminal half; ATP-bindings sites (`Walker'-motifs A and B, and motif C) are highlighted (Confalonieri and Duguet, 1995). Below, the deletion constructs S4-I to S4-V in pJG are shown. Numbers refer to included codons. (D) Interactions of Pros26.4 deletion constructs and Hairless HFL in pEG were quantified: only S4-I, which contains the N-terminal half but lacks the ATPase domain, retains its binding activity, which is in contrast with any of the other constructs. Control was empty vector (pEG). (E) Co-immunoprecipitation of Pros26.4 and Hairless from embryonic extracts. Protein extracts from Drosophila embryos were taken for immunoprecipitation using anti-Hairless antiserum (IP H). Precipitates were probed with either Hairless antiserum (left) or Pros26.4 antiserum (anti-S4; right). For comparison, total embryonic extracts were loaded in the next lane (in, input about 12% of IP). As control (co), the precipitation was performed with unrelated antiserum. Molecular mass is given in kDa.

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