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Molecular and Cellular Biology, August 1999, p. 5486-5494, Vol. 19, No. 8
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Human TAFII55 Interacts with the Vitamin D3 and Thyroid Hormone Receptors and with Derivatives of the Retinoid X Receptor That Have Altered Transactivation Properties

Anne-Claire Lavigne, Gabrielle Mengus,dagger Yann-Gaël Gangloff, Jean-Marie Wurtz, and Irwin Davidson*

Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, Illkirch Cédex, C.U. de Strasbourg, France

Received 9 October 1998/Returned for modification 14 December 1998/Accepted 14 May 1999

We have identified novel interactions between the human (h)TATA-binding protein-associated factor TAFII55 and the ligand-binding domains (LBDs) of the nuclear receptors for vitamin D3 (VDR) and thyroid hormone (TRalpha ). Following expression in Cos cells, hTAFII55 interacts with the VDR and TRalpha LBDs in a ligand-independent manner whereas no interactions with the retinoid X receptors (RXRs) or with other receptors were observed. Deletion mapping indicates that hTAFII55 interacts with a 40-amino-acid region spanning alpha -helices H3 to H5 of the VDR and TRalpha LBDs but not with the equivalent highly related region of RXRgamma . TAFII55 also interacts with chimeric receptors in which the H3-to-H5 region of RXRgamma has been replaced with that of the VDR or TRalpha . Furthermore, replacement of two single amino acids of the RXRgamma LBD with their VDR counterparts allows the RXRgamma LBD to interact with hTAFII55 while the corresponding double substitution allows a much stronger interaction. In transfection experiments, the single mutated RXRgamma LBDs activate transcription to fivefold higher levels than wild-type RXRgamma while the double mutation activates transcription to a level comparable to that observed with the VDR. There is therefore a correlation between the ability of the modified RXRs to interact with hTAFII55 and transactivation. These results strongly suggest that the TAFII55 interactions with the modified RXR LBDs modulate transcriptional activation.

* Corresponding author. Mailing address: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, B.P. 163-67404, Illkirch Cédex, C.U. de Strasbourg, France. Phone: 33 3 88 65 34 40 (45). Fax: 33 3 88 65 32 01. E-mail: irwin{at}titus.u-strasbg.fr.

dagger Present address: EMBL, 69012, Heidelberg, Germany.

Molecular and Cellular Biology, August 1999, p. 5486-5494, Vol. 19, No. 8
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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