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J Biol Chem, Vol. 274, Issue 43, 30402-30409, October 22, 1999

Conservation and Divergence of the Yeast and Mammalian Unfolded Protein Response
ACTIVATION OF SPECIFIC MAMMALIAN ENDOPLASMIC RETICULUM STRESS ELEMENT OF THE grp78/BiP PROMOTER BY YEAST Hac1

Dolly M. Foti, Ajith Welihinda^§, Randal J. Kaufman^§, and Amy S. Lee

From the  Department of Biochemistry and Molecular Biology and the University of Southern California/Norris Comprehensive Cancer Center, University of Southern California School of Medicine, Los Angeles, California 90089 and the ^§ Department of Biological Chemistry, and the Howard Hughes Medical Institute, University of Michigan Medical School, Ann Arbor, Michigan 48109

Yeast Hac1 (yHac1), the transcription factor that binds and activates the unfolded protein response element of endoplasmic reticulum (ER)-chaperone gene promoters, only accumulates in stressed cells after an unconventional splicesosome-free mRNA processing step and escape from translation block. In determining whether the novel regulatory mechanisms for yHac1 are conserved in mammalian cells, we discovered a unique unfolded protein response element-like sequence within the endoplasmic reticulum stress element 163, one of the three ER stress elements recently identified in the rat grp78 promoter. The unspliced form of yHac1 is stably expressed in nonstressed mammalian cells and is as active as the spliced form in stimulating the promoter activities of grp genes. Further, the yHac1 mRNA is not processed in response to ER stress in mammalian cells. We identified a CCAGC motif as the yHac1 binding site, which is contained within a YY1 binding site previously shown to be important for mammalian UPR. Dissection of the yHac1 and the YY1 binding sites uncovered specific contact points for an activator protein predicted to be the mammalian homolog of yHac1, the activity of which can be stimulated by YY1. A model of the conserved and unique features of the yeast and mammalian unfolded protein response transcription machinery is proposed.

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