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Fig. 9. (A) Gene structure of rib. The salient features of the longest cDNA (3959 nt; BDGP LD16058) are depicted, and the position of the single intron is noted. A consensus polyadenylation signal (AATAAA) is present near the end of the 3' UTR. By northern analysis, we detected a single transcript of 4.3 kb (data not shown), which correlates well with cDNA length and suggests the cDNA is nearly full length. (B) Conceptual translation of the 1963 nt ORF yields a 661-residue protein. Translation of the corresponding GadFly gene CG7230 reveals an identical protein sequence. An N-terminal BTB/POZ domain is denoted in bold. There are four consensus NLSs (underlined). A predicted coiled-coil region in the C terminus is double underlined. RIB contains seven MAPK consensus phosphorylation sites (PX1-2S/TP, where X is any amino acid), which are boxed. The mutations in rib1 and rib2 alleles are double-boxed: rib1 encodes a stop codon after residue 282, and rib2 has an arginine to histidine substitution at residue 58 (R58H). (C) Sequence alignment of the RIB BTB/POZ domain with BTB/POZ domains of Drosophila Longitudinals lacking (LOLA), Drosophila Bric a brac (BAB), mouse Zinc finger protein 161 (mZfp161), and human Promyelocytic leukemia zinc finger (hPLZF). The eleven N-terminal residues (under the bar) are not included in the BTB/POZ domain as defined by the InterPro program; however, this short stretch is highly conserved in these three and other Drosophila BTB/POZ domain proteins. Percentage identity and similarity of the BTB/POZ domains with respect to RIB are noted. Residues that were examined in a structure/function analysis of hPLZF (Melnick et al., 2000) are indicated by an open circle, and residues that, when mutated, disrupt BTB/POZ domain function are also indicated by a filled circle. Note that the rib2 allele has a change in one of these essential residues (*). Black shading, white letters denotes identical residues; dark gray shading, white letters denotes conserved residues; grey shading denotes similar residues.