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Nucleic Acids Research, 1990, Vol. 18, No. 19 5853-5863
© 1990
MOLECULAR BIOLOGY |
A distal dimerization domain is essential for DNA-binding by the atypical HNF1 homeodomain
Unité des virus oncogènes UA 1149 du CNRS, Département de Biologie Moléculaire, Institut Pasteur 25 rue du Dr Roux, 75724 Paris cedex 15, France 1Laboratotium voor Genetica Rijksuniversiteit Gent, B 9000 Gent, Belgium
* To whom correspondence should be addressed
Received March 8, 1990. Revised August 8, 1990. Accepted August 8, 1990.
Hepatic Nuclear Factor 1 (HNF1, also referred to as LFB1, HP1 or APF) is a liver-specific transcnption factor required for the expression of many hepatocyte specific genes. We report here the purification of this rat liver nuclear protein and the cloning of its cDNA using a PCR-derived approach. Seven independent clones reveal 3 alternative polyadenylation sites and a unique open reading frame. Both a motif homologous to the homeodomain and a distal dimerization domain are required for specific DNA binding. Sequence comparisons reveal several atypical features at key positions in the segment corresponding to helices III and IV of the Antaennapedia homeodomain as well as a potential 24 amino acid loop in place of the universal turn between helices II and III. Together with its property to dimerize in the presence or absence of DNA, these features place HNF1 as the prototype of a novel subclass of transcription factors distantly related homeoproteins.
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