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An upstream regulatory element of the NCAM promoter contains a binding site for homeodomains
Author(s) -
Hirsch Marie-Rose,
Valarché Isabelle,
Deagostini-Bazin Hermine,
Pernelle Christine,
Joliot Alain,
Goridis Christo
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80050-d
Subject(s) - upstream (networking) , binding site , biology , chemistry , genetics , computer science , computer network
In the present study, we have analyzed an upstream regulatory element of the neural cell adhesion molecule (NCAM) promoter which is required for full promoter activity. It contains an ATTATTA motif that resembles the core recognition sequence of homeodomain (HD) proteins of the Antennapedia (Antp) and related types. Electrophoretic mobility shift (EMSA) and DNase I footprinting analyses revealed that the Drosophila HDs coded by the Antp and the zerknüllt (zen) genes bind this site in vitro. In contrast, the engrailed (en) protein did not produce a detectable footprint. The functional relevance of the ATTATTA motif was demonstrated by showing that a two‐nucleotide exchange curtailed stimulation of an heterologous promotor. An oligonucleotide known to be recognized with high affinity by Antp ‐like HDs efficiently competed for endogenous factor binding. These results suggest that the NCAM gene may be a target for HD proteins.