Biochem Biophys Res Commun. 2000 Jul 5;273(2):596-602.

Cloning of a coproporphyrinogen oxidase promoter regulatory element binding protein.

Takahashi S, Furuyama K, Kobayashi A, Taketani S, Harigae H, Yamamoto M, Igarashi K, Sasaki T, Hayashi N.

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Department of Biochemistry, Tohoku University School of Medicine, Sendai, 980-8575, Japan.

Abstract

Coproporphyrinogen oxidase [CPO] gene promoter regulatory element (CPRE) plays an important role in CPO gene regulation. To isolate a CPRE binding protein, we performed Southwestern screening of K562 cDNA expression library using CPRE as a probe and isolated a cDNA clone which encoded a novel protein, Klp1 (K562 cell-derived leucine-zipper-like protein 1). Klp1 mRNA was highly expressed in K562 cells, HeLa cells, and brain as a single transcript (1.4 kb). Gel mobility shift assays revealed that Klp1 specifically binds to CPRE. Computational analysis revealed that Klp1 has a leucine-zipper-like structure, a Leu-X-X-Leu-Leu motif, and a putative nuclear localization signal in the basic amino acid rich region. Transfection of the Klp1 expression vector into THP-1 cells resulted in transcriptional activation of a reporter construct containing CPRE. These results indicate that Klp1 is a DNA sequence-specific transcription factor that regulates gene expression of genes that contain CPRE in their regulatory region.

PMID:: 10873651; [PubMed - indexed for MEDLINE]

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