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Nucleic Acids Research, 1991, Vol. 19, No. 5 1121-1127
© 1991

MOLECULAR BIOLOGY

Cloning and sequence analysis of TFE, a helix-loop-helix transcription factor able to recognize the thyroglobulin gene promoter in vitro

Françoise Javaux, Alena Donda, Gilbert Vassart1 and Daniel Christophe

1Department of genetics, Université Libre de Bruxelles Campus Erasme, 808 Route de Lennik, 1070 Brussels, Belgium IRIBHN Université Libre de Bruxelles Campus Erasme, 808 Route de Lennik, 1070 Brussels, Belgium

Received September 30, 1990. Revised January 31, 1991. Accepted January 31, 1991.

A cDNA that encodes a transcription factor able to recognize the thyroglobulin gene promoter in vitro was isolated from a dog thyroid cDNA expression library In {lambda}gt11. The library was screened with a multimerized 20 bp-oligonucleotide probe corresponding to the –126 to –107 bp region of the bovine thyroglobulin gene promoter. The specificity of DNA sequence recognition was demonstrated by DNA binding experiments realized with ß-galactosidase-fusion protein immobilized on nitrocellulose filters and various unlabelled multimerized competing DNA fragments. The encoded protein, TFE, appears to be the canine counterpart of a recently cloned human transcription factor, ITF-2, that binds to the µE5xE2 motif found in both Immunoglobulin heavy and light chains genes enhancers and belongs to the basic-Helix-Loop-Helix family of transcription factors. When TFE protein was produced in a rabbit reticulocyte lysate, It displayed the same specificity of DNA sequence recognition as the ß-galactosidase fusion protein and immobilization of the translation product on nitrocellulose still appeared to be essential for detecting in vitro DNA binding activity. Functional data failed to assign a role for TFE in the control of thyroglobulin gene transcription in vitro, suggesting that the selection of TFE clone resulted from the fortuitous presence of a high affinity binding site in the probe used for screening the expression library.


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