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Volume 271, Number 27, Issue of July 5, 1996 pp. 16008-16019
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Characterization of a Polypyrimidine/Polypurine Tract in the Promoter of the Gene for Chicken Malic Enzyme

(Received for publication, March 5, 1996, and in revised form, April 23, 1996)

From the Department of Biochemistry, University of Iowa, Iowa City, Iowa 52240

Starvation inhibits and refeeding stimulates transcription of the malic enzyme gene in chick liver. DNA between 320 and +72 base pairs (bp) is DNase I-hypersensitive in hepatic nuclei from fed but not starved chicks (Ma, X. J., and Goodridge, A. G. (1992) Nucleic Acids Res. 20, 4997-5002). A polypyrimidine/polypurine (PPY/PPU) tract lies within the DNase I-hypersensitive region. In hepatocytes transiently transfected with plasmids containing triiodothyronine response elements and a minimal promoter from the malic enzyme gene linked to the chloramphenicol acetyltransferase gene, deletion of the PPY/PPU tract inhibited chloramphenicol acetyltransferase activity by about 90% with or without triiodothyronine. Fine mapping of S1 nuclease-sensitive sites suggests that the PPY/PPU tract can assume different isoforms of non-B-DNA, some of which may be triplex structures. The PPY/PPU tract contains specific binding sites for single- and double-stranded DNA binding proteins and, with 8 bp 3 of the tract, can function as a promoter. A (CT)₇ repeat binds single-stranded DNA-binding protein and is essential for promoter activity. Two C-rich elements bind single-stranded DNA-binding proteins and may mediate inhibition of promoter function. The single- and double-stranded DNA-binding proteins that interact with the PPY/PPU tract may regulate transcription of the malic enzyme gene.

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