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Insulin gene enhancer binding protein Isl-1 is a member of a novel class of proteins containing both a homeo-and a Cys–His domain

Abstract

THE activity of the rat insulin I gene enhancer is mainly dependent on two cis-acting protein-binding domains1–3. Here we report the isolation of a complementary DNA encoding a protein, Isl-1, that binds to one of these domains. Isl-1 contains a homeodomain with greatest similarity to those of the Caenorhabditis elegans proteins encoded by mec-3 (ref. 4) and lin-11 (ref. 5). In addition, Isl-1, like the lin-11 and mec-3 gene products, contains a novel Cys–His domain which is reminiscent of known metal-binding regions. Together these proteins define a novel class of proteins containing both a homeo- and a Cys His–domain. Isl-1 is preferentially expressed in cells of pancreatic endocrine origin. If the structural homologies between Isl-1 and the C. elegans gene products reflect functional similarities, a role for Isl-1 in the development of pancreatic endocrine cells could be envisaged.

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Karlsson, O., Thor, S., Norberg, T. et al. Insulin gene enhancer binding protein Isl-1 is a member of a novel class of proteins containing both a homeo-and a Cys–His domain. Nature 344, 879–882 (1990). https://doi.org/10.1038/344879a0

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