Nucleic Acids Research, Vol 25, Issue 8 1476-1484, Copyright © 1997 by Oxford University Press
DJ Sourdive, C Transy, S Garbay and M Yaniv
HNF1 is a liver enriched atypical homeoprotein isolated from vertebrates
which is involved in the transcriptional activation of liver, kidney,
intestine and pancreas specific genes. HNF1 contains an N-terminal
dimerisation and a POU-like domain both essential together with the
homeodomain for DNA specific recognition. Using the yeast two- hybrid
system we searched for proteins interacting with HNF1. We repeatedly
obtained cDNA clones encoding DCOH/4-alpha-carbinolamine dehydratase, an
enzyme involved in the oxidation of aromatic amino acids that was shown to
bind to and stabilise HNF1 dimers. Using the yeast system, we show that the
enzymatic activity of DCOH is not essential for HNF1 binding and that the
HNF1 dimerisation domain is sufficient for DCOH binding. Furthermore we
demonstrate that both proteins co-localise in co-transfected cells.
ARTICLES
The bifunctional DCOH protein binds to HNF1 independently of its 4- alpha-carbinolamine dehydratase activity
Unite des Virus Oncogenes, URA 1644 du CNRS, Departement des Biotechnologies, U163 INSERM, Institut Pasteur, 25, rue du Dr Roux, 75724 Paris cedex 15, France.
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