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J. Biol. Chem., Vol. 277, Issue 17, 14564-14574, April 26, 2002
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From the Thyroid transcription factor 1 (TTF-1) is a
homeodomain-containing transcriptional regulator responsible for the
activation of thyroid- and lung-specific genes. It has been
demonstrated that its DNA binding activity is redox-regulated in
vitro through the formation of dimers and oligomeric species. In
this paper, we demonstrate that the redox regulation mainly involves a
Cys residue (Cys87), which resides out of the DNA binding
domain, belonging to the N-transactivation domain. In fact, the
oxidized form of a truncated TTF-1 (containing the N-transactivation
domain and the DNA-binding domain, here called TTF-1N-HD) looses
specific DNA binding activity. Since most of the oxidized TTF-1N-HD is
in a monomeric form, these data indicate that the redox state of
Cys87 may control the DNA-binding function of the
homeodomain, suggesting that Cys87 could play an important
role in determining the correct folding of the homeodomain. By using
gel retardation and transient transfection assays, we demonstrate that
the redox effector factor-1 (Ref-1) mediates the redox effects on
TTF-1N-HD binding and that it is able to modulate the TTF-1
transcriptional activity. Glutathione S-transferase
pull-down experiments demonstrate the occurrence of interaction between
Ref-1 and TTF-1N-HD. Having previously demonstrated that Ref-1 is able
to modulate the transcriptional activity of another thyroid-specific
transcription factor (Pax-8), our data suggest that Ref-1 plays a
central role in the regulation of thyroid cells.
Redox Effector Factor-1 Regulates the Activity of Thyroid
Transcription Factor 1 by Controlling the Redox State of the N
Transcriptional Activation Domain*
§,,,
,, and Dipartimento di Biochimica, Biofisica e
Chimica delle Macromolecole, via Giorgieri 1, Università degli
Studi di Trieste, Trieste 34127, Italy, the ¶ Dipartimento di
Scienze e Tecnologie Biomediche, P. le Kolbe 1, Università degli
Studi di Udine, Udine 33100, Italy, and the Department of
Biochemistry and Molecular Biology, Indiana University School of
Medicine, Indianapolis, Indiana 46202
*
This work was supported by grant "Progetto Giovani
Ricercatori 2000" from the University of Trieste (to G. T.) and by
grants from the Consiglio Nazionale delle Ricerche (Target Project on Biotechnology) and from MURST (to G. D.). The costs of this
publication of this article were defrayed in part by the payment of
page charges. This article must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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