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J Biol Chem, Vol. 273, Issue 47, 31442-31448, November 20, 1998

Cross-talk between Orphan Nuclear Hormone Receptor RZR and Peroxisome Proliferator-activated Receptor  in Regulation of the Peroxisomal Hydratase-Dehydrogenase Gene

Christopher J. Winrow, John P. Capone^¶, and Richard A. Rachubinski

From the  Department of Cell Biology and Anatomy, University of Alberta, Edmonton, Alberta T6G 2H7 and the ^¶ Department of Biochemistry, McMaster University, Hamilton, Ontario L8N 3Z5, Canada

The genes encoding the peroxisomal -oxidation enzymes enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD) and fatty acyl-CoA oxidase (AOx) are coordinately regulated by peroxisome proliferator-activated receptor  (PPAR)/9-cis-retinoic acid receptor (RXR) heterodimers that transactivate these genes in a ligand-dependent manner via upstream peroxisome proliferator response elements (PPRE). Here we demonstrate that the monomeric orphan nuclear hormone receptor, RZR, modulates PPAR/RXR-dependent transactivation in a response-element dependent manner. Electrophoretic mobility shift analysis showed that RZR bound specifically as a monomer to the HD-PPRE but not the AOx-PPRE. Determinants in the HD-PPRE for binding of RZR were distinct from those required for interaction with PPAR/RXR heterodimers. In transient transfections, RZR stimulated ligand-mediated transactivation by PPAR from an HD-PPRE luciferase reporter in the absence of exogenously added RXR, but did not affect PPAR-dependent transactivation of an AOx-PPRE reporter gene. These data illustrate cross-talk between the RZR and PPAR signaling pathways at the level of the HD-PPRE in the regulation of the HD gene and characterize additional factors governing the regulation of peroxisomal -oxidation.

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