Interaction between the retinoid X receptor and transcription factor IIB is ligand-dependent in vivo.

The Journal of Biological Chemistry
G M LeongJ H Segars

Abstract

The retinoid X receptor (RXR) influences gene activation through heterodimeric and homodimeric association with DNA and associates with TATA binding protein, TAF110, and cAMP response element-binding protein-binding protein; yet the molecular mechanisms responsible for gene activation by RXRs remain incompletely defined. Since the general transcription factor IIB (TFIIB) is a common target of sequence-specific transcriptional activators, we suspected that RXR might regulate target genes via an interaction with TFIIB. Coimmunoprecipitation, far Western analysis, and glutathione S-transferase binding studies indicated that murine RXR beta (mRXR beta) was capable of binding to human TFIIB in vitro. Functional analysis with a dual-hybrid yeast system and cotransfection assays revealed the interaction of mRXR beta with TFIIB to be ligand-dependent in vivo. Truncation experiments mapped the essential binding regions to the carboxyl region of mRXR beta (amino acids (aa) 254-389) and two regions in the carboxyl region of TFIIB (aa 178-201 and aa 238-271). Furthermore, the delta 390-410 mRXR beta mutant bound to TFIIB in vitro but was not active in the dual-hybrid yeast system, suggesting that the extreme carboxyl region of RXR was requ...Continue Reading

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Citations

May 30, 2001·Molecular and Biochemical Parasitology·M R FantappieP T LoVerde
May 15, 2002·Journal of Bone and Mineral Research : the Official Journal of the American Society for Bone and Mineral Research·Laura L IssaJohn A Eisman
Mar 19, 1999·Molecular and Cellular Biology·T MiyamotoK Hashizume
Jan 17, 2003·The Journal of Biological Chemistry·Janelle B BarryEdith M Gardiner

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