NOVEL CYSTEINE-RICH MOTIF AND HOMEODOMAIN IN THE PRODUCT OF THE CAENORHABDITIS-ELEGANS CELL LINEAGE GENE LIN-II

THE genelin-11 is required for the asymmetric division of a vulval precursor cell type in the nematode Caenorhabditis elegans. Putative lin-11 complementary DNAs were sequenced and found to encode a protein that contains both a homeodomain and two tandem copies of a novel cysteine-rich motif: C-X2-C-X17-19-H-X2-C-X2-C-X 2-C-X7-11-(C)-X8-C. Two tandem copies of this motif are also present amino-terminal to the homeodomains in the proteins encoded by the genes mec-3, which is required for C. elegans touch neuron differentiation1, and isl-1, which encodes a rat insulin I gene enhancer-binding protein2. The arrangement of cysteine residues in this motif, referred to as LIM (for lin-11 isl-1 mec-3), suggests that this region is a metal-binding domain. The presence in these three proteins of both a potential metal-binding domain and a homeodomain distinguishes them from previously characterized proteins. © 1990 Nature Publishing Group.