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© Research
Publication : Nucleic acids research

The bifunctional DCOH protein binds to HNF1 independently of its 4-alpha-carbinolamine dehydratase activity

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Nucleic acids research - 15 Apr 1997

Sourdive DJ, Transy C, Garbay S, Yaniv M

Link to Pubmed [PMID] – 9092652

Nucleic Acids Res. 1997 Apr;25(8):1476-84

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.

http://www.ncbi.nlm.nih.gov/pubmed/9092652