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Molecular and Cellular Biology, May 2001, p. 3220-3233, Vol. 21, No. 9
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.9.3220-3233.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Identification of TFII-I as the Endoplasmic Reticulum Stress Response Element Binding Factor ERSF: Its Autoregulation by Stress and Interaction with ATF6

Ronald Parker,1 Trevor Phan,1 Peter Baumeister,1 Binayak Roy,1 Venugopalan Cheriyath,2 Ananda L. Roy,2 and Amy S. Lee1,*

Department of Biochemistry and Molecular Biology and the USC/Norris Comprehensive Cancer Center, Keck School of Medicine of the University of Southern California, Los Angeles, California 90089-9176,1 and Department of Pathology and Programs in Immunology and Genetics, Tufts University School of Medicine, Boston, Massachusetts 021112

Received 4 October 2000/Returned for modification 1 December 2000/Accepted 29 January 2001

When mammalian cells are subjected to stress targeted to the endoplasmic reticulum (ER), such as depletion of the ER Ca2+ store, the transcription of a family of glucose-regulated protein (GRP) genes encoding ER chaperones is induced. The GRP promoters contain multiple copies of the ER stress response element (ERSE), consisting of a unique tripartite structure, CCAAT(N9)CCACG. Within a subset of mammalian ERSEs, N9 represents a GC-rich sequence of 9 bp that is conserved across species. A novel complex (termed ERSF) exhibits enhanced binding to the ERSE of the grp78 and ERp72 promoters using HeLa nuclear extracts prepared from ER-stressed cells. Optimal binding of ERSF to ERSE and maximal ERSE-mediated stress inducibility require the conserved GGC motif within the 9-bp region. Through chromatographic purification and subsequent microsequencing, we have identified ERSF as TFII-I. Whereas TFII-I remains predominantly nuclear in both nontreated NIH 3T3 cells and cells treated with thapsigargin (Tg), a potent inducer of the GRP stress response through depletion of the ER Ca2+ store, the level of TFII-I transcript was elevated in Tg-stressed cells, correlating with an increase in TFII-I protein level in the nuclei of Tg-stressed cells. Purified recombinant TFII-I isoforms bind directly to the ERSEs of grp78 and ERp72 promoters. The stimulation of ERSE-mediated transcription by TFII-I requires the consensus tyrosine phosphorylation site of TFII-I and the GGC sequence motif of the ERSE. We further discovered that TFII-I is an interactive protein partner of ATF6 and that optimal stimulation of ERSE by ATF6 requires TFII-I.

* Corresponding author. Mailing address: USC/Norris Comprehensive Cancer Center, 1441 Eastlake Ave., Room 5308, MC-9176, Los Angeles, CA 90089-9176. Phone: (323) 865-0507. Fax: (323) 865-0094. E-mail: amylee{at}hsc.usc.edu.

Molecular and Cellular Biology, May 2001, p. 3220-3233, Vol. 21, No. 9
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.9.3220-3233.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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