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Volume 271, Number 48, Issue of November 29, 1996 pp. 30886-30896
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Isolation and Expression of cDNAs from Rainbow Trout (Oncorhynchus mykiss) That Encode Two Novel Basic Helix-Loop-Helix/PER-ARNT-SIM (bHLH/PAS) Proteins with Distinct Functions in the Presence of the Aryl Hydrocarbon Receptor
EVIDENCE FOR ALTERNATIVE mRNA SPLICING AND DOMINANT NEGATIVE ACTIVITY IN THE bHLH/PAS FAMILY

(Received for publication, July 12, 1996, and in revised form, September 17, 1996)

Richard S. Pollenz , Hillary R. Sullivan , Jennifer Holmes , Brian Necela and Richard E. Peterson ^¶

From the  Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425 and the ^¶ Environmental Toxicology Center and School of Pharmacy, University of Wisconsin, Madison, Wisconsin 53706

cDNAs encoding two distinct basic helix-loop-helix/PER-ARNT-SIM (bHLH/PAS) proteins with similarity to the mammalian aryl hydrocarbon nuclear translocator (ARNT) protein were isolated from RTG-2 rainbow trout gonad cells. The deduced proteins, termed rtARNT_a and rtARNT_b, are identical over the first 533 amino acids and contain a basic helix-loop-helix domain that is 100% identical to human ARNT. rtARNT_a and rtARNT_b differ in their COOH-terminal domains due to the presence of an additional 373 base pairs of sequence that have the characteristics of an alternatively spliced exon. The presence of the 373-base pair region causes a shift in the reading frame. rtARNT_a lacks the sequence and has a COOH-terminal domain of 104 residues rich in proline, serine, and threonine. rtARNT_b contains the sequence and has a COOH-terminal domain of 190 residues rich in glutamine and asparagine. mRNAs for both rtARNT splice variants were detected in RTG-2 gonad cells, trout liver, and gonad tissue. rtARNT_a and rtARN_b protein were identified in cell lysates from RTG-2 cells. Transfection of rtARNT expression vectors into murine Hepa-1 cells that are defective in ARNT function (type II) result in rtARNT protein expression localized to the nucleus. Treatment of these cells with 2,3,7,8-tetrachlorodibenzo-p-dioxin results in a 20-fold greater induction of endogenous P4501A1 protein in cells expressing rtARNT_b when compared with rtARNT_a, even though both proteins effectively dimerize with the aryl hydrocarbon receptor. The decreased function of rtARNT_a appears to be due to inefficient binding of rtARNT_a·AHR complexes to DNA. In addition, the presence of rtARNT_a can reduce the aryl hydrocarbon receptor-dependent function of rtARNT_b in vivo and in vitro.

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